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Record Information
Version3.6
Creation Date2006-08-16 13:51:54 UTC
Update Date2014-08-06 17:54:10 UTC
HMDB IDHMDB01361
Secondary Accession NumbersNone
Metabolite Identification
Common NameCarbon monoxide
DescriptionCarbon monoxide, with the chemical formula CO, is a colorless, odorless, and tasteless gas. It is the product of the incomplete combustion of carbon-containing compounds, notably in internal-combustion engines. It consists of one carbon atom covalently bonded to one oxygen atom. It is a gas at room temperature. Carbon monoxide is a significantly toxic gas and is the most common type of fatal poisoning in many countries. Exposures can lead to significant toxicity of the central nervous system and heart. Carbon monoxide has a higher diffusion coefficient compared to oxygen and the only enzyme in the human body that produces carbon monoxide is heme oxygenase which is located in all cells and breaks down heme. Because it has a higher diffusion coefficient than oxygen the body easily gets rid of any CO made. When CO is not ventilated it binds to hemoglobin, which is the principal oxygen-carrying compound in blood; this produces a compound known as carboxyhemoglobin. The traditional belief is that carbon monoxide toxicity arises from the formation of carboxyhemoglobin, which decreases the oxygen-carrying capacity of the blood and inhibits the transport, delivery, and utilization of oxygen by the body. The affinity between hemoglobin and carbon monoxide is approximately 230 times stronger than the affinity between hemoglobin and oxygen so hemoglobin binds to carbon monoxide in preference to oxygen. Following poisoning, long-term sequelae often occur. Carbon monoxide can also have severe effects on the fetus of a pregnant woman. Despite its serious toxicity, CO is extremely useful and underpins much modern technology, being a precursor to a myriad of useful - even life-saving - products. Carbon monoxide, though thought of as a pollutant today, has always been present in the atmosphere, chiefly as a product of volcanic activity. It occurs dissolved in molten volcanic rock at high pressures in the earth's mantle. Carbon monoxide contents of volcanic gases vary from less than 0.01% to as much as 2% depending on the volcano. It also occurs naturally in bushfires. Because natural sources of carbon monoxide are so variable from year to year, it is extremely difficult to accurately measure natural emissions of the gas. (wikipedia).
Structure
Thumb
Synonyms
  1. Carbon monoxide
  2. CO
Chemical FormulaCO
Average Molecular Weight28.0101
Monoisotopic Molecular Weight27.994914622
IUPAC NameNot Available
Traditional IUPAC NameNot Available
CAS Registry NumberNot Available
SMILES
[C]#[O]
InChI Identifier
InChI=1S/CO/c1-2
InChI KeyUGFAIRIUMAVXCW-UHFFFAOYSA-N
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassAliphatic Acyclic Compounds
ClassN/A
Sub ClassN/A
Other Descriptors
  • a small molecule(Cyc)
  • carbon oxide(ChEBI)
Substituents
  • N/A
Direct ParentAliphatic Acyclic Compounds
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Component of Porphyrin and chlorophyll metabolism
ApplicationNot Available
Cellular locations
  • Cytoplasm
  • Extracellular
Physical Properties
StateLiquid
Experimental Properties
PropertyValueReference
Melting Point-56.5 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility1.48 mg/mL at 25 °CNot Available
LogP0.83HANSCH,C ET AL. (1995)
Predicted Properties
PropertyValueSource
water solubility5.11 g/LALOGPS
logP-0.73ALOGPS
logS-0.75ALOGPS
physiological charge0ChemAxon
hydrogen acceptor count0ChemAxon
hydrogen donor count0ChemAxon
polar surface area0ChemAxon
rotatable bond count0ChemAxon
refractivity26.23ChemAxon
polarizability1.94ChemAxon
Spectra
SpectraNot Available
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
Biofluid Locations
  • Blood
Tissue LocationNot Available
PathwaysNot Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified72.0 +/- 25.0 uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified350.0 +/- 178.0 uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease References
Smoking
  1. Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Associated OMIM IDsNone
DrugBank IDNot Available
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB022578
KNApSAcK IDNot Available
Chemspider ID275
KEGG Compound IDC00237
BioCyc IDNot Available
BiGG ID1749973
Wikipedia LinkCarbon monoxide
NuGOwiki LinkHMDB01361
Metagene LinkHMDB01361
METLIN IDNot Available
PubChem Compound281
PDB IDCMO
ChEBI ID17245
References
Synthesis ReferenceIvanova, Svetlana; Pitchon, Veronique; Petit, Corinne. Application of the direct exchange method in the preparation of gold catalysts supported on different oxide materials. Journal of Molecular Catalysis A: Chemical (2006), 256(1-2), 278-283.
Material Safety Data Sheet (MSDS)Not Available
General ReferencesNot Available

Enzymes

General function:
Involved in heme oxygenase (decyclizing) activity
Specific function:
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
Gene Name:
HMOX2
Uniprot ID:
P30519
Molecular weight:
36032.615
Reactions
Hemoglobin + FADH + Oxygen → Globin + Biliverdin + Carbon monoxide + Fe3+ + FAD + Waterdetails
General function:
Involved in heme oxygenase (decyclizing) activity
Specific function:
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
Gene Name:
HMOX1
Uniprot ID:
P09601
Molecular weight:
32818.345
Reactions
Hemoglobin + FADH + Oxygen → Globin + Biliverdin + Carbon monoxide + Fe3+ + FAD + Waterdetails
General function:
Involved in monooxygenase activity
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. This enzyme requires molecular oxygen and NADPH for the omega-hydroxylation of LTB4, a potent chemoattractant for polymorphonuclear leukocytes.
Gene Name:
CYP4F3
Uniprot ID:
Q08477
Molecular weight:
59846.085
General function:
Involved in ion channel activity
Specific function:
Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX)
Gene Name:
KCNMA1
Uniprot ID:
Q12791
Molecular weight:
137558.1
General function:
Involved in protein serine/threonine kinase activity
Specific function:
Mediates down-regulation of protein synthesis in response to various stress conditions by the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51'. Protein synthesis is inhibited at the level of initiation
Gene Name:
EIF2AK1
Uniprot ID:
Q9BQI3
Molecular weight:
71105.9
General function:
Involved in metal ion binding
Specific function:
Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Also down-regulates cell migration mediated by MMP14. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line.
Gene Name:
ADI1
Uniprot ID:
Q9BV57
Molecular weight:
21498.23
Reactions
1,2-Dihydroxy-3-keto-5-methylthiopentene + Oxygen → 3-Methylthiopropionic acid + Formic acid + Carbon monoxidedetails