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Record Information
Version2.0
Creation Date2009-03-06 18:58:18 UTC
Update Date2014-12-24 20:21:20 UTC
Accession NumberT3D0215
Identification
Common NameChromic acid
ClassSmall Molecule
DescriptionChromic acid generally refers to a collection of compounds generated by the acidification of solutions containing chromate and dichromate anions or the dissolving of chromium trioxide in sulfuric acid. Chromic acid contains hexavalent chromium. Hexavalent chromium refers to chromium in the +6 oxidation state, and is more toxic than other oxidation states of the chromium atom because of its greater ability to enter cells and a higher redox potential. (9) Molecular chromic acid, H2CrO4, has much in common with sulfuric acid, H2SO4 as both are classified as strong acids. Chromic acid was widely used in the instrument repair industry, due to its ability to "brighten" raw brass. A chromic acid dip leaves behind a bright yellow patina on the brass. Due to growing health and environmental concerns, many have discontinued use of this chemical in their repair shops. Most chromic acid sold or available as a 10% aqueous solution.
Compound Type
  • Chromium Compound
  • Industrial/Workplace Toxin
  • Inorganic Compound
  • Pollutant
  • Synthetic Compound
Chemical Structure
Thumb
Synonyms
Synonym
Chromate
Chromic Acid
Chromium hydroxide oxide
Dihydrogen(tetraaoxidochromate)
Dihydroxidodioxidochromium
H2CrO4
Tetraoxochromic acid
[CrO2(OH)2]
Chemical FormulaCrH2O4
Average Molecular Mass118.010 g/mol
Monoisotopic Mass117.936 g/mol
CAS Registry Number7738-94-5
IUPAC Namedioxochromiumdiol
Traditional Namechromic acid
SMILESO[Cr](O)(=O)=O
InChI IdentifierInChI=1S/Cr.2H2O.2O/h;2*1H2;;/q+2;;;;/p-2
InChI KeyInChIKey=KRVSOGSZCMJSLX-UHFFFAOYSA-L
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as miscellaneous chromates. These are inorganic compounds in which the largest metallic oxoanion is chromate, to which either no atom or a non metal atom is bonded.
KingdomInorganic compounds
Super ClassMixed metal/non-metal compounds
ClassMiscellaneous mixed metal/non-metals
Sub ClassMiscellaneous metallic oxoanionic compounds
Direct ParentMiscellaneous chromates
Alternative Parents
Substituents
  • Chromate
  • Inorganic oxide
  • Inorganic salt
Molecular FrameworkNot Available
External Descriptors
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Membrane
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical Roles
Physical Properties
StateSolid or Liquid
AppearanceRed powder; Orange liquid (acid)
Experimental Properties
PropertyValue
Melting Point197°C (solid)
Boiling Point100°C (acid); 250°C (solid)
SolubilityNot Available
LogPNot Available
Predicted Properties
PropertyValueSource
logP-2.5ChemAxon
pKa (Strongest Acidic)11.81ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area74.6 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity8.02 m³·mol⁻¹ChemAxon
Polarizability6.51 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-014i-0900000000-f339e8b185b6511879a0JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-014i-0900000000-0ffb6d3c099fe25d4838JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-014i-1900000000-0652730d77e7f81111f0JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-014i-0900000000-2b794de366bf8de77cf3JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-014i-1900000000-5a683e4c85e8b7dc2182JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-014i-0900000000-82a448a699a8ecda2657JSpectraViewer
Toxicity Profile
Route of ExposureOral (8) ; inhalation (8) ; dermal (8)
Mechanism of ToxicityChromic acid is highly corrosive and strongly oxidative. Many strong acids cause tissue burns through the denaturation of proteins and partial hydrolysis of proteins. Most proteins denature at pH values of less than 3-4. The large-scale denaturation of proteins, de-esterification of lipids and subsequent desiccation of tissues leads to chemical burns. . Symptoms include itching, bleaching or darkening of skin or tissues, blistering and burning sensations. Chromic acid also denatures proteins through inserting oxygen atoms into protein side chains. Chromic acid is also a source of chromium and especially hexavalent chromium. Hexavalent chromium compounds (including chromium trioxide, chromic acids, chromates, chlorochromates) are toxic and carcinogenic. For this reason, chromic acid oxidation is not used on an industrial scale except in the aerospace industry. Hexavalent chromium's carcinogenic effects are caused by its metabolites, pentavalent and trivalent chromium. The DNA damage may be caused by hydroxyl radicals produced during reoxidation of pentavalent chromium by hydrogen peroxide molecules present in the cell. Trivalent chromium may also form complexes with peptides, proteins, and DNA, resulting in DNA-protein crosslinks, DNA strand breaks, DNA-DNA interstrand crosslinks, chromium-DNA adducts, chromosomal aberrations and alterations in cellular signaling pathways. It has been shown to induce carcinogenesis by overstimulating cellular regulatory pathways and increasing peroxide levels by activating certain mitogen-activated protein kinases. It can also cause transcriptional repression by cross-linking histone deacetylase 1-DNA methyltransferase 1 complexes to CYP1A1 promoter chromatin, inhibiting histone modification. Chromium may increase its own toxicity by modifying metal regulatory transcription factor 1, causing the inhibition of zinc-induced metallothionein transcription. (1, 8, 2, 3, 4)
MetabolismSkin contact with chromic acid can cause redness, pain, and severe skin burns. Chromic acid may cause severe burns to the eye and permanent eye damage. Severe and rapid corrosive burns of the mouth, gullet and gastrointestinal tract will result if chromic acid is swallowed. Symptoms include burning, choking, nausea, vomiting and severe pain. Chronic exposure to low levels of chromic acid can lead to chronic exposure to hexavalent chromium. Hexavalent chromium is a known carcinogen. Chronic inhalation especially has been linked to lung cancer. Hexavalent chromium is also known to cause reproductive and developmental defects. (1)
Toxicity ValuesLD50: 330 mg/kg (Oral, Dog) (6)
Lethal Dose1 to 3 grams for an adult human (hexavalent chromium). (5)
Carcinogenicity (IARC Classification)1, carcinogenic to humans. (12)
Uses/SourcesChromic acid is an intermediate in chromium plating, and is also used in ceramic glazes, and colored glass. (10)
Minimum Risk LevelIntermediate Oral: 0.005 mg/kg/day (11) Chronic Oral: 0.001 mg/kg/day (11)
Health EffectsSkin contact with chromic acid can cause redness, pain, and severe skin burns. Chromic acid may cause severe burns to the eye and permanent eye damage. Severe and rapid corrosive burns of the mouth, gullet and gastrointestinal tract will result if chromic acid is swallowed. Symptoms include burning, choking, nausea, vomiting and severe pain. Chronic exposure to low levels of chromic acid can lead to chronic exposure to hexavalent chromium. Hexavalent chromium is a known carcinogen. Chronic inhalation especially has been linked to lung cancer. Hexavalent chromium is also known to cause reproductive and developmental defects. (1)
SymptomsSkin contact can cause redness, pain, and severe skin burns. Chromic acid may cause severe burns to the eye and permanent eye damage. Severe and rapid corrosive burns of the mouth, gullet and gastrointestinal tract will result if chromic acid is swallowed. Symptoms include burning, choking, nausea, vomiting and severe pain.
TreatmentThe mainstay of treatment of any acid burn is copious irrigation with large amounts of tap water. To be most effective, treatment should be started immediately after exposure, preferably before arrival in the emergency department. Remove any contaminated clothing. Do not attempt to neutralize the burn with weak reciprocal chemicals (i.e. alkali for acid burns), because the heat generated from the chemical reaction may cause severe thermal injury.
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDNot Available
HMDB IDNot Available
PubChem Compound ID24425
ChEMBL IDNot Available
ChemSpider ID22834
KEGG IDNot Available
UniProt IDNot Available
OMIM ID
ChEBI ID33143
BioCyc IDNot Available
CTD IDNot Available
Stitch IDChromic acid
PDB IDNot Available
ACToR ID7935
Wikipedia LinkNot Available
References
Synthesis ReferenceNot Available
MSDST3D0215.pdf
General References
  1. Salnikow K, Zhitkovich A: Genetic and epigenetic mechanisms in metal carcinogenesis and cocarcinogenesis: nickel, arsenic, and chromium. Chem Res Toxicol. 2008 Jan;21(1):28-44. Epub 2007 Oct 30. [17970581 ]
  2. Kim G, Yurkow EJ: Chromium induces a persistent activation of mitogen-activated protein kinases by a redox-sensitive mechanism in H4 rat hepatoma cells. Cancer Res. 1996 May 1;56(9):2045-51. [8616849 ]
  3. Schnekenburger M, Talaska G, Puga A: Chromium cross-links histone deacetylase 1-DNA methyltransferase 1 complexes to chromatin, inhibiting histone-remodeling marks critical for transcriptional activation. Mol Cell Biol. 2007 Oct;27(20):7089-101. Epub 2007 Aug 6. [17682057 ]
  4. Kimura T: [Molecular mechanism involved in chromium(VI) toxicity]. Yakugaku Zasshi. 2007 Dec;127(12):1957-65. [18057785 ]
  5. Barceloux DG: Chromium. J Toxicol Clin Toxicol. 1999;37(2):173-94. [10382554 ]
  6. Folli C, Viglione S, Busconi M, Berni R: Biochemical basis for retinol deficiency induced by the I41N and G75D mutations in human plasma retinol-binding protein. Biochem Biophys Res Commun. 2005 Nov 4;336(4):1017-22. [16157297 ]
  7. Sax NI (1987). Dangerous Properties of Industrial Materials Reports. New York: Van Nostrand Rheinhold.
  8. ATSDR - Agency for Toxic Substances and Disease Registry (2008). Toxicological profile for chromium. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  9. Wikipedia. Chromic acid. Last Updated 11 March 2009. [Link]
  10. ATSDR - Agency for Toxic Substances and Disease Registry (1997). Toxicological profile for tetrachloroethylene (PERC) . U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  11. 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]
  12. International Agency for Research on Cancer (2014). IARC Monographs on the Evaluation of Carcinogenic Risks to Humans. [Link]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available

Targets

General Function:
Transcription regulatory region sequence-specific dna binding
Specific Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.
Gene Name:
HDAC1
Uniprot ID:
Q13547
Molecular Weight:
55102.615 Da
References
  1. Schnekenburger M, Talaska G, Puga A: Chromium cross-links histone deacetylase 1-DNA methyltransferase 1 complexes to chromatin, inhibiting histone-remodeling marks critical for transcriptional activation. Mol Cell Biol. 2007 Oct;27(20):7089-101. Epub 2007 Aug 6. [17682057 ]
2. DNA
General Function:
Used for biological information storage.
Specific Function:
DNA contains the instructions needed for an organism to develop, survive and reproduce.
Molecular Weight:
2.15 x 1012 Da
References
  1. ATSDR - Agency for Toxic Substances and Disease Registry (2008). Toxicological profile for chromium. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
General Function:
Transcriptional activator activity, rna polymerase ii core promoter proximal region sequence-specific binding
Specific Function:
Activates the metallothionein I promoter. Binds to the metal responsive element (MRE).
Gene Name:
MTF1
Uniprot ID:
Q14872
Molecular Weight:
80956.22 Da
References
  1. Kimura T: [Molecular mechanism involved in chromium(VI) toxicity]. Yakugaku Zasshi. 2007 Dec;127(12):1957-65. [18057785 ]
General Function:
Rna polymerase ii carboxy-terminal domain kinase activity
Specific Function:
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation.Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity.
Gene Name:
MAPK1
Uniprot ID:
P28482
Molecular Weight:
41389.265 Da
References
  1. Kim G, Yurkow EJ: Chromium induces a persistent activation of mitogen-activated protein kinases by a redox-sensitive mechanism in H4 rat hepatoma cells. Cancer Res. 1996 May 1;56(9):2045-51. [8616849 ]
General Function:
Phosphatase binding
Specific Function:
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade.
Gene Name:
MAPK3
Uniprot ID:
P27361
Molecular Weight:
43135.16 Da
References
  1. Kim G, Yurkow EJ: Chromium induces a persistent activation of mitogen-activated protein kinases by a redox-sensitive mechanism in H4 rat hepatoma cells. Cancer Res. 1996 May 1;56(9):2045-51. [8616849 ]