Barium cyanide (T3D1103)

IdentificationTaxonomyBiological PropertiesPhysical PropertiesToxicity ProfileSpectraConcentrationsLinksReferencesGene RegulationTargets (63)XML
Targets (63)
Record Information
Version2.0
Creation Date2009-06-19 21:58:18 UTC
Update Date2014-12-24 20:23:09 UTC
Accession NumberT3D1103
Identification
Common NameBarium cyanide
ClassSmall Molecule
DescriptionBarium cyanide is a chemical compound of barium and cyanide. Barium is a metallic alkaline earth metal with the symbol Ba, and atomic number 56. It never occurs in nature in its pure form due to its reactivity with air, but combines with other chemicals such as sulfur or carbon and oxygen to form barium compounds that may be found as minerals. (5)
Compound Type
  • Barium Compound
  • Cyanide Compound
  • Industrial/Workplace Toxin
  • Inorganic Compound
  • Pollutant
  • Synthetic Compound
Chemical Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
Synonym
Ba(CN)2
Barium dicyanide
Chemical FormulaC2BaN2
Average Molecular Mass189.362 g/mol
Monoisotopic Mass189.911 g/mol
CAS Registry Number542-62-1
IUPAC Namebarium(2+) ion bis(iminomethanide)
Traditional Namebarium(2+) ion bis(cyanide)
SMILES[Ba++].[C-]#N.[C-]#N
InChI IdentifierInChI=1S/2CN.Ba/c2*1-2;/q2*-1;+2
InChI KeyInChIKey=UNLSXXHOHZUADN-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as alkaline earth metal nitrides. These are inorganic compounds of nitrogen where nitrogen has a formal oxidation state of -3, and the heaviest metal atom is an alkaline earth metal.
KingdomInorganic compounds
Super ClassMixed metal/non-metal compounds
ClassAlkaline earth metal organides
Sub ClassAlkaline earth metal nitrides
Direct ParentAlkaline earth metal nitrides
Alternative Parents
Substituents
  • Alkaline earth metal nitride
  • Inorganic nitride
  • Inorganic salt
  • Inorganic cyanide
Molecular FrameworkNot Available
External DescriptorsNot Available
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Cytoplasm
  • Extracellular
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Physical Properties
StateSolid
AppearanceWhite powder.
Experimental Properties
PropertyValue
Melting Point600°C
Boiling PointNot Available
SolubilityNot Available
LogPNot Available
Predicted Properties
PropertyValueSource
Water Solubility33.2 g/LALOGPS
logP-0.48ALOGPS
logP-0.35ChemAxon
logS-0.76ALOGPS
pKa (Strongest Acidic)9.5ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count1ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area23.79 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity15.81 m³·mol⁻¹ChemAxon
Polarizability2.07 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
SpectraNot Available
Toxicity Profile
Route of ExposureOral (2) ; inhalation (2) ; dermal (2)
Mechanism of ToxicityBarium is a competitive potassium channel antagonist that blocks the passive efflux of intracellular potassium, resulting in a shift of potassium from extracellular to intracellular compartments. The intracellular translocation of potassium results in a decreased resting membrane potential, making the muscle fibers electrically unexcitable and causing paralysis. Some of these barium's effects may also be due to barium induced neuromuscular blockade and membrane depolarization. Cyanide is an inhibitor of cytochrome c oxidase in the fourth complex of the electron transport chain (found in the membrane of the mitochondria of eukaryotic cells). It complexes with the ferric iron atom in this enzyme. The binding of cyanide to this cytochrome prevents transport of electrons from cytochrome c oxidase to oxygen. As a result, the electron transport chain is disrupted and the cell can no longer aerobically produce ATP for energy. Tissues that mainly depend on aerobic respiration, such as the central nervous system and the heart, are particularly affected. Cyanide is also known produce some of its toxic effects by binding to catalase, glutathione peroxidase, methemoglobin, hydroxocobalamin, phosphatase, tyrosinase, ascorbic acid oxidase, xanthine oxidase, succinic dehydrogenase, and Cu/Zn superoxide dismutase. Cyanide binds to the ferric ion of methemoglobin to form inactive cyanmethemoglobin. (3, 5)
MetabolismBarium compounds are absorbed via ingestion and inhalation, the extent of which depends on the individual compound. In the body, the majority of the barium is found in the bone, while small amounts exists in the muscle, adipose, skin, and connective tissue. Barium is not metabolized in the body, but it may be transported or incorporated into complexes or tissues. Barium is excreted in the urine and faeces. Cyanide is rapidly alsorbed through oral, inhalation, and dermal routes and distributed throughout the body. Cyanide is mainly metabolized into thiocyanate by either rhodanese or 3-mercaptopyruvate sulfur transferase. Cyanide metabolites are excreted in the urine. (2, 5)
Toxicity ValuesNot Available
Lethal Dose1 to 15 grams for an adult human (barium salts). (1)
Carcinogenicity (IARC Classification)No indication of carcinogenicity to humans (not listed by IARC).
Uses/SourcesNot Available
Minimum Risk LevelIntermediate Oral: 0.2 mg/kg/day (Barium) (4) Chronic Oral: 0.2 mg/kg/day (Barium) (4) Acute Inhalation: 0.00003 mg/m3 (Cadmium) (4) Chronic Inhalation: 0.00001 mg/m3 (Cadmium) (4) Intermediate Oral: 0.0005 mg/kg/day (Cadmium) (4) Chronic Oral: 0.0001 mg/kg/day (Cadmium) (4)
Health EffectsThe health effects of the different barium compounds depend on how well the compound dissolves in water or the stomach contents. At low doses, barium acts as a muscle stimulant, while higher doses affect the nervous system, causing cardiac irregularities, tremors, weakness, anxiety, dyspnea, paralysisand possibly death. Barium may also cause gastrointestinal disturbances, damage the kidneys and cause decreases in body weight. Exposure to high levels of cyanide for a short time harms the brain and heart and can even cause coma, seizures, apnea, cardiac arrest and death. Chronic inhalation of cyanide causes breathing difficulties, chest pain, vomiting, blood changes, headaches, and enlargement of the thyroid gland. Skin contact with cyanide salts can irritate and produce sores. (2, 3, 5)
SymptomsIngesting excess barium may cause vomiting, abdominal cramps, diarrhea, difficulties in breathing, increased or decreased blood pressure, numbness around the face, and muscle weakness. High levels may result in changes in heart rhythm or paralysis and possibly death. Cyanide poisoning is identified by rapid, deep breathing and shortness of breath, general weakness, giddiness, headaches, vertigo, confusion, convulsions/seizures and eventually loss of consciousness. (2, 3, 5)
TreatmentIntravenous infusion of potassium often relieves many of the symptoms of barium toxicity. Antidotes to cyanide poisoning include hydroxocobalamin and sodium nitrite, which release the cyanide from the cytochrome system, and rhodanase, which is an enzyme occurring naturally in mammals that combines serum cyanide with thiosulfate, producing comparatively harmless thiocyanate. Oxygen therapy can also be administered. (3, 5)
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDNot Available
HMDB IDNot Available
PubChem Compound ID6093184
ChEMBL IDNot Available
ChemSpider IDNot Available
KEGG IDNot Available
UniProt IDNot Available
OMIM ID
ChEBI IDNot Available
BioCyc IDNot Available
CTD IDNot Available
Stitch IDBarium cyanide
PDB IDNot Available
ACToR ID6374
Wikipedia LinkNot Available
References
Synthesis ReferenceNot Available
MSDST3D1103.pdf
General References
  1. Gosselin RE, Smith RP, and Hodge HC (1984). Clinical Toxicology of Commercial Products. 5th ed. Baltimore: Williams and Wilkins.
  2. ATSDR - Agency for Toxic Substances and Disease Registry (2006). Toxicological profile for cyanide. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  3. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
  4. ATSDR - Agency for Toxic Substances and Disease Registry (2001). Minimal Risk Levels (MRLs) for Hazardous Substances. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  5. ATSDR - Agency for Toxic Substances and Disease Registry (2007). Toxicological profile for barium. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available

Targets

Target Details
1. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
General Function:
Succinate dehydrogenase activity
Specific Function:
Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor.
Gene Name:
SDHA
Uniprot ID:
P31040
Molecular Weight:
72690.975 Da
References
  1. Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
  2. Bolognesi M, Rosano C, Losso R, Borassi A, Rizzi M, Wittenberg JB, Boffi A, Ascenzi P: Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study. Biophys J. 1999 Aug;77(2):1093-9. [10423453 ]
Target Details
2. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
General Function:
Ubiquinone binding
Specific Function:
Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHB
Uniprot ID:
P21912
Molecular Weight:
31629.365 Da
References
  1. Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
  2. Bolognesi M, Rosano C, Losso R, Borassi A, Rizzi M, Wittenberg JB, Boffi A, Ascenzi P: Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study. Biophys J. 1999 Aug;77(2):1093-9. [10423453 ]
Target Details
3. ATP-sensitive inward rectifier potassium channel 1
General Function:
Phosphatidylinositol-4,5-bisphosphate binding
Specific Function:
In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
Gene Name:
KCNJ1
Uniprot ID:
P48048
Molecular Weight:
44794.6 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
4. ATP-sensitive inward rectifier potassium channel 11
General Function:
Voltage-gated potassium channel activity
Specific Function:
This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium (By similarity). Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation.
Gene Name:
KCNJ11
Uniprot ID:
Q14654
Molecular Weight:
43540.375 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
5. ATP-sensitive inward rectifier potassium channel 12
General Function:
Inward rectifier potassium channel activity
Specific Function:
Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
Gene Name:
KCNJ12
Uniprot ID:
Q14500
Molecular Weight:
49000.6 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
6. ATP-sensitive inward rectifier potassium channel 8
General Function:
Inward rectifier potassium channel activity
Specific Function:
This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium (By similarity).
Gene Name:
KCNJ8
Uniprot ID:
Q15842
Molecular Weight:
47967.455 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
7. ATP-sensitive potassium channel (Protein Group)
General Function:
Phosphatidylinositol-4,5-bisphosphate binding
Specific Function:
In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
Included Proteins:
P48048 , P78508 , Q14654 , Q14500 , Q9UNX9 , Q99712 , Q15842
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
8. ATP-sensitive potassium channel (Protein Group)
General Function:
Phosphatidylinositol-4,5-bisphosphate binding
Specific Function:
In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
Included Proteins:
P48048 , P78508 , Q14654 , Q14500 , Q9UNX9 , Q99712 , Q15842
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
9. ATP-sensitive potassium channel (Protein Group)
General Function:
Phosphatidylinositol-4,5-bisphosphate binding
Specific Function:
In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
Included Proteins:
P48048 , P78508 , Q14654 , Q14500 , Q9UNX9 , Q99712 , Q15842
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
10. Alkaline phosphatase, placental-like
General Function:
Metal ion binding
Specific Function:
Not Available
Gene Name:
ALPPL2
Uniprot ID:
P10696
Molecular Weight:
57376.515 Da
References
  1. Gerbitz KD: Human alkaline phosphatases. II. Metalloenzyme properties of the enzyme from human liver. Hoppe Seylers Z Physiol Chem. 1977 Nov;358(11):1491-7. [924371 ]
Target Details
11. Alkaline phosphatase, tissue-nonspecific isozyme
General Function:
Pyrophosphatase activity
Specific Function:
This isozyme may play a role in skeletal mineralization.
Gene Name:
ALPL
Uniprot ID:
P05186
Molecular Weight:
57304.435 Da
References
  1. Gerbitz KD: Human alkaline phosphatases. II. Metalloenzyme properties of the enzyme from human liver. Hoppe Seylers Z Physiol Chem. 1977 Nov;358(11):1491-7. [924371 ]
Target Details
12. Calmodulin
General Function:
Titin binding
Specific Function:
Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.
Gene Name:
CALM1
Uniprot ID:
P0DP23
Molecular Weight:
16837.47 Da
References
  1. Kursula P, Majava V: A structural insight into lead neurotoxicity and calmodulin activation by heavy metals. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt 8):653-6. Epub 2007 Jul 28. [17671360 ]
Target Details
13. Catalase
General Function:
Receptor binding
Specific Function:
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.
Gene Name:
CAT
Uniprot ID:
P04040
Molecular Weight:
59755.82 Da
References
  1. Kang YS, Lee DH, Yoon BJ, Oh DC: Purification and characterization of a catalase from photosynthetic bacterium Rhodospirillum rubrum S1 grown under anaerobic conditions. J Microbiol. 2006 Apr;44(2):185-91. [16728955 ]
Target Details
14. Cytochrome c oxidase subunit 1
General Function:
Iron ion binding
Specific Function:
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Gene Name:
MT-CO1
Uniprot ID:
P00395
Molecular Weight:
57040.91 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
15. Cytochrome c oxidase subunit 2
General Function:
Cytochrome-c oxidase activity
Specific Function:
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.
Gene Name:
MT-CO2
Uniprot ID:
P00403
Molecular Weight:
25564.73 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
16. Cytochrome c oxidase subunit 3
General Function:
Cytochrome-c oxidase activity
Specific Function:
Subunits I, II and III form the functional core of the enzyme complex.
Gene Name:
MT-CO3
Uniprot ID:
P00414
Molecular Weight:
29950.6 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
17. Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX4I1
Uniprot ID:
P13073
Molecular Weight:
19576.6 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
18. Cytochrome c oxidase subunit 4 isoform 2, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX4I2
Uniprot ID:
Q96KJ9
Molecular Weight:
20010.02 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
19. Cytochrome c oxidase subunit 5A, mitochondrial
General Function:
Metal ion binding
Specific Function:
This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX5A
Uniprot ID:
P20674
Molecular Weight:
16761.985 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
20. Cytochrome c oxidase subunit 5B, mitochondrial
General Function:
Metal ion binding
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX5B
Uniprot ID:
P10606
Molecular Weight:
13695.57 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
21. Cytochrome c oxidase subunit 6A1, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX6A1
Uniprot ID:
P12074
Molecular Weight:
12154.8 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
22. Cytochrome c oxidase subunit 6A2, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX6A2
Uniprot ID:
Q02221
Molecular Weight:
10815.32 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
23. Cytochrome c oxidase subunit 6B1
General Function:
Cytochrome-c oxidase activity
Specific Function:
Connects the two COX monomers into the physiological dimeric form.
Gene Name:
COX6B1
Uniprot ID:
P14854
Molecular Weight:
10192.345 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
24. Cytochrome c oxidase subunit 6B2
General Function:
Cytochrome-c oxidase activity
Specific Function:
Connects the two COX monomers into the physiological dimeric form.
Gene Name:
COX6B2
Uniprot ID:
Q6YFQ2
Molecular Weight:
10528.905 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
25. Cytochrome c oxidase subunit 6C
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX6C
Uniprot ID:
P09669
Molecular Weight:
8781.36 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
26. Cytochrome c oxidase subunit 7A1, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX7A1
Uniprot ID:
P24310
Molecular Weight:
9117.44 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
27. Cytochrome c oxidase subunit 7A2, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX7A2
Uniprot ID:
P14406
Molecular Weight:
9395.89 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
28. Cytochrome c oxidase subunit 7B, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Plays a role in proper central nervous system (CNS) development in vertebrates.
Gene Name:
COX7B
Uniprot ID:
P24311
Molecular Weight:
9160.485 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
29. Cytochrome c oxidase subunit 7B2, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX7B2
Uniprot ID:
Q8TF08
Molecular Weight:
9077.43 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
30. Cytochrome c oxidase subunit 7C, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX7C
Uniprot ID:
P15954
Molecular Weight:
7245.45 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
31. Cytochrome c oxidase subunit 8A, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX8A
Uniprot ID:
P10176
Molecular Weight:
7579.0 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
32. Cytochrome c oxidase subunit 8C, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Gene Name:
COX8C
Uniprot ID:
Q7Z4L0
Molecular Weight:
8128.575 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
33. Epididymal secretory glutathione peroxidase
General Function:
Glutathione peroxidase activity
Specific Function:
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.
Gene Name:
GPX5
Uniprot ID:
O75715
Molecular Weight:
25202.14 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
34. Extracellular superoxide dismutase [Cu-Zn]
General Function:
Zinc ion binding
Specific Function:
Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Gene Name:
SOD3
Uniprot ID:
P08294
Molecular Weight:
25850.675 Da
References
  1. Lee WG, Hwang JH, Na BK, Cho JH, Lee HW, Cho SH, Kong Y, Song CY, Kim TS: Functional expression of a recombinant copper/zinc superoxide dismutase of filarial nematode, Brugia malayi. J Parasitol. 2005 Feb;91(1):205-8. [15856906 ]
Target Details
35. G protein-activated inward rectifier potassium channel 1
General Function:
G-protein activated inward rectifier potassium channel activity
Specific Function:
This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.
Gene Name:
KCNJ3
Uniprot ID:
P48549
Molecular Weight:
56602.84 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
36. G protein-activated inward rectifier potassium channel 2
General Function:
Inward rectifier potassium channel activity
Specific Function:
This potassium channel may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters acting through G-protein-coupled receptors. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
Gene Name:
KCNJ6
Uniprot ID:
P48051
Molecular Weight:
48450.96 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
37. G protein-activated inward rectifier potassium channel 3
General Function:
G-protein activated inward rectifier potassium channel activity
Specific Function:
This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium (By similarity).
Gene Name:
KCNJ9
Uniprot ID:
Q92806
Molecular Weight:
44019.45 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
38. G protein-activated inward rectifier potassium channel 4
General Function:
G-protein activated inward rectifier potassium channel activity
Specific Function:
This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium.
Gene Name:
KCNJ5
Uniprot ID:
P48544
Molecular Weight:
47667.3 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
39. Glutathione peroxidase 1
General Function:
Sh3 domain binding
Specific Function:
Protects the hemoglobin in erythrocytes from oxidative breakdown.
Gene Name:
GPX1
Uniprot ID:
P07203
Molecular Weight:
22087.94 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
40. Glutathione peroxidase 2
General Function:
Glutathione peroxidase activity
Specific Function:
Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors.
Gene Name:
GPX2
Uniprot ID:
P18283
Molecular Weight:
21953.835 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
41. Glutathione peroxidase 3
General Function:
Transcription factor binding
Specific Function:
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
Gene Name:
GPX3
Uniprot ID:
P22352
Molecular Weight:
25552.185 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
42. Glutathione peroxidase 6
General Function:
Glutathione peroxidase activity
Specific Function:
Not Available
Gene Name:
GPX6
Uniprot ID:
P59796
Molecular Weight:
24970.46 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
43. Glutathione peroxidase 7
General Function:
Peroxidase activity
Specific Function:
It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks.
Gene Name:
GPX7
Uniprot ID:
Q96SL4
Molecular Weight:
20995.88 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
44. Glutathione reductase, mitochondrial
General Function:
Nadp binding
Specific Function:
Maintains high levels of reduced glutathione in the cytosol.
Gene Name:
GSR
Uniprot ID:
P00390
Molecular Weight:
56256.565 Da
References
  1. Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
Target Details
45. Hemoglobin subunit alpha
General Function:
Oxygen transporter activity
Specific Function:
Involved in oxygen transport from the lung to the various peripheral tissues.
Gene Name:
HBA1
Uniprot ID:
P69905
Molecular Weight:
15257.405 Da
References
  1. Bolognesi M, Rosano C, Losso R, Borassi A, Rizzi M, Wittenberg JB, Boffi A, Ascenzi P: Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study. Biophys J. 1999 Aug;77(2):1093-9. [10423453 ]
Target Details
46. Hemoglobin subunit beta
General Function:
Oxygen transporter activity
Specific Function:
Involved in oxygen transport from the lung to the various peripheral tissues.LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.Spinorphin: functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation.
Gene Name:
HBB
Uniprot ID:
P68871
Molecular Weight:
15998.34 Da
References
  1. Bolognesi M, Rosano C, Losso R, Borassi A, Rizzi M, Wittenberg JB, Boffi A, Ascenzi P: Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study. Biophys J. 1999 Aug;77(2):1093-9. [10423453 ]
Target Details
47. Inward rectifier potassium channel 13
General Function:
Inward rectifier potassium channel activity
Specific Function:
Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium.
Gene Name:
KCNJ13
Uniprot ID:
O60928
Molecular Weight:
40529.195 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
48. Inward rectifier potassium channel 16
General Function:
Inward rectifier potassium channel activity
Specific Function:
Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ16 may be involved in the regulation of fluid and pH balance.
Gene Name:
KCNJ16
Uniprot ID:
Q9NPI9
Molecular Weight:
47948.585 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
49. Inward rectifier potassium channel 2
General Function:
Voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization
Specific Function:
Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium or cesium.
Gene Name:
KCNJ2
Uniprot ID:
P63252
Molecular Weight:
48287.82 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
50. Inward rectifier potassium channel 4
General Function:
Pdz domain binding
Specific Function:
Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity).
Gene Name:
KCNJ4
Uniprot ID:
P48050
Molecular Weight:
49499.61 Da
References
  1. Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
Target Details
51. Phospholipid hydroperoxide glutathione peroxidase, mitochondrial
General Function:
Phospholipid-hydroperoxide glutathione peroxidase activity
Specific Function:
Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage.
Gene Name:
GPX4
Uniprot ID:
P36969
Molecular Weight:
22174.52 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
52. Potassium voltage-gated channel subfamily KQT member 1
General Function:
Voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization
Specific Function:
Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity) (PubMed:10646604). Associates with KCNE beta subunits that modulates current kinetics (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505, PubMed:19687231). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (PubMed:10713961). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (PubMed:10646604). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms an heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (PubMed:11101505). When associated with KCNE4, inhibits voltage-gated potassium channel activity (PubMed:19687231). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (PubMed:12324418). Also forms an heterotetramer with KCNQ5; has a voltage-gated potassium channel activity (PubMed:24855057). Binds with phosphatidylinositol 4,5-bisphosphate (PubMed:25037568).Isoform 2: Non-functional alone but modulatory when coexpressed with the full-length isoform 1.
Gene Name:
KCNQ1
Uniprot ID:
P51787
Molecular Weight:
74697.925 Da
References
  1. Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
Target Details
53. Potassium voltage-gated channel subfamily KQT member 2
General Function:
Voltage-gated potassium channel activity
Specific Function:
Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. KCNQ2/KCNQ3 current is blocked by linopirdine and XE991, and activated by the anticonvulsant retigabine. Muscarinic agonist oxotremorine-M strongly suppress KCNQ2/KCNQ3 current in cells in which cloned KCNQ2/KCNQ3 channels were coexpressed with M1 muscarinic receptors.
Gene Name:
KCNQ2
Uniprot ID:
O43526
Molecular Weight:
95846.575 Da
References
  1. Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
Target Details
54. Potassium voltage-gated channel subfamily KQT member 3
General Function:
Voltage-gated potassium channel activity
Specific Function:
Probably important in the regulation of neuronal excitability. Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs.
Gene Name:
KCNQ3
Uniprot ID:
O43525
Molecular Weight:
96741.515 Da
References
  1. Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
Target Details
55. Potassium voltage-gated channel subfamily KQT member 4
General Function:
Potassium channel activity
Specific Function:
Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. KCNQ4 channels are blocked by linopirdin, XE991 and bepridil, whereas clofilium is without significant effect. Muscarinic agonist oxotremorine-M strongly suppress KCNQ4 current in CHO cells in which cloned KCNQ4 channels were coexpressed with M1 muscarinic receptors.
Gene Name:
KCNQ4
Uniprot ID:
P56696
Molecular Weight:
77099.99 Da
References
  1. Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
Target Details
56. Potassium voltage-gated channel subfamily KQT member 5
General Function:
Voltage-gated potassium channel activity
Specific Function:
Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. Muscarine suppresses KCNQ5 current in Xenopus oocytes in which cloned KCNQ5 channels were coexpressed with M(1) muscarinic receptors.
Gene Name:
KCNQ5
Uniprot ID:
Q9NR82
Molecular Weight:
102178.015 Da
References
  1. Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
Target Details
57. Probable glutathione peroxidase 8
General Function:
Peroxidase activity
Specific Function:
Not Available
Gene Name:
GPX8
Uniprot ID:
Q8TED1
Molecular Weight:
23880.83 Da
References
  1. Kraus RJ, Ganther HE: Reaction of cyanide with glutathione peroxidase. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1116-22. [7437059 ]
Target Details
58. Putative cytochrome c oxidase subunit 7A3, mitochondrial
General Function:
Cytochrome-c oxidase activity
Specific Function:
Not Available
Gene Name:
COX7A2P2
Uniprot ID:
O60397
Molecular Weight:
11840.715 Da
References
  1. Wikipedia. Cyanide poisoning. Last Updated 30 March 2009. [Link]
Target Details
59. Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
General Function:
Ubiquinone binding
Specific Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHD
Uniprot ID:
O14521
Molecular Weight:
17042.82 Da
References
  1. Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
Target Details
60. Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
General Function:
Succinate dehydrogenase activity
Specific Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHC
Uniprot ID:
Q99643
Molecular Weight:
18610.03 Da
References
  1. Ardelt BK, Borowitz JL, Isom GE: Brain lipid peroxidation and antioxidant protectant mechanisms following acute cyanide intoxication. Toxicology. 1989 Jun 1;56(2):147-54. [2734799 ]
Target Details
61. Superoxide dismutase [Cu-Zn]
General Function:
Zinc ion binding
Specific Function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Gene Name:
SOD1
Uniprot ID:
P00441
Molecular Weight:
15935.685 Da
References
  1. Lee WG, Hwang JH, Na BK, Cho JH, Lee HW, Cho SH, Kong Y, Song CY, Kim TS: Functional expression of a recombinant copper/zinc superoxide dismutase of filarial nematode, Brugia malayi. J Parasitol. 2005 Feb;91(1):205-8. [15856906 ]
Target Details
62. Tyrosinase
General Function:
Protein homodimerization activity
Specific Function:
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.
Gene Name:
TYR
Uniprot ID:
P14679
Molecular Weight:
60392.69 Da
References
  1. Laufer Z, Beckett RP, Minibayeva FV: Co-occurrence of the multicopper oxidases tyrosinase and laccase in lichens in sub-order peltigerineae. Ann Bot. 2006 Nov;98(5):1035-42. Epub 2006 Sep 1. [16950829 ]
Target Details
63. Xanthine dehydrogenase/oxidase
General Function:
Xanthine oxidase activity
Specific Function:
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro).
Gene Name:
XDH
Uniprot ID:
P47989
Molecular Weight:
146422.99 Da
References
  1. Bolognesi M, Rosano C, Losso R, Borassi A, Rizzi M, Wittenberg JB, Boffi A, Ascenzi P: Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study. Biophys J. 1999 Aug;77(2):1093-9. [10423453 ]