World Library  
Flag as Inappropriate
Email this Article

Carbon monoxide dehydrogenase

Article Id: WHEBN0014132547
Reproduction Date:

Title: Carbon monoxide dehydrogenase  
Author: World Heritage Encyclopedia
Language: English
Subject: Wood–Ljungdahl pathway
Collection:
Publisher: World Heritage Encyclopedia
Publication
Date:
 

Carbon monoxide dehydrogenase

carbon-monoxide dehydrogenase (acceptor)
Identifiers
EC number CAS number IntEnz BRENDA ExPASy KEGG MetaCyc metabolic pathway
PRIAM PDB structures PDBsum
Gene Ontology EGO

In chemical reaction

CO + H2O + A \rightleftharpoons CO2 + AH2

The 3 substrates of this enzyme are CO, H2O, and A, whereas its two products are CO2 and AH2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is carbon-monoxide:acceptor oxidoreductase. Other names in common use include anaerobic carbon monoxide dehydrogenase, carbon monoxide oxygenase, carbon-monoxide dehydrogenase, and carbon-monoxide:(acceptor) oxidoreductase.

Classes

Two major classes of the carbon monoxide dehydrogenase (CODH) enzymes have been identified. CODH containing a Mo-[2Fe-2S]-FAD active site have been found in aerobic bacteria, while a distinct class of Ni-[3Fe-4S] CODH enzymes have been purified from anaerobic bacteria.[1][2] Both classes of CODH catalyze the reversible conversion between carbon dioxide (CO2) and carbonmonoxide (CO). CODH exists in both monofuctional and bifunctional forms. In the latter case, CODH forms a bifunctional cluster with acetyl-CoA synthase, as has been well characterized in the anaerobic bacteria Moorella thermoacetica.[3][4]

Structure


Multiple research groups have proposed crystal structures for the α2β2 tetrameric enzyme CODH/ACS from the acetogenic bacteria M. thermoacetica, including two recent examples since 2009:

A noteworthy feature of the M.thermoacetica CODH/ACS is an internal gas tunnel connecting the multiple active sites.[5] The full role of the gas channel in regulating the rate catalytic activity is still a subject of investigation, but several studies support the notion that molecules of CO do in fact travel directly from the C-cluster to the ACS active site without leaving the enzyme. For instance, the rate of acetyl-CoA synthase activity in the bifunctional enzyme is not affected by the addition of hemoglobin, which would compete for CO in bulk solution,[6] and isotopic labeling studies show that carbon monoxide derived from the C-cluster is preferentially used at the A-cluster over unlabeled CO in solution.[7] Protein engineering of the CODH/ACS in M.thermoacetica revealed that mutating residues, so as to functionally block the tunnel, stopped acety-CoA synthesis when only CO2 was present.[8] The discovery of a functional CO tunnel places CODH on a growing list of enzymes that independently evolved this strategy to transfer reactive intermediates from one active site to another.[9]

As of late 2007, 13 1ZXI.

Reaction mechanisms

Oxidative mechanism

The CODH catalytic site, referred to as the C-cluster, is a [3Fe-4S] cluster bonded to a Ni-Fe moiety. Two basic amino acids (Lys587 and His 113 in M.thermoacetica) reside in proximity to the C-cluster and facilitate acid-base chemistry required for enzyme activity.[10] Based on IR spectra suggesting the presence of an Ni-CO complex, the proposed first step in the oxidative catalysis of CO to CO2 involves the binding of CO to Ni2+ and corresponding complexing of Fe2+ to a water molecule.[11] The binding of CO molecule causes a shift in the coordination of the Ni atom from a square-planar to square pyramidal geometry.[12] Dobbek et al. further propose that movement of the Nickel atom’s cysteine ligand brings the CO into close proximity to the hydroxyl group, and facilitate a base-catalyzed, nucleophillic attack by the iron-bound hydroxy group. A carboxy bridge between the Ni and Fe atom has been proposed as an intermediate. [13] A decarboxylation leads to the release of CO2 and the reduction of the cluster. Although the resulting intermediate oxidation state of the Ni and the degree to which electrons are distributed throughout the Ni-[3Fe-4S] cluster is subject of some debate, the electrons in the reduced C-cluster are transferred to nearby B and D [4Fe-4S] clusters, returning the Ni-[3Fe-4S] C-cluster to an oxidized state and reducing the single electron carrier ferredoxin.[14]

Reductive mechanism

Given CODH's role in CO2 fixation identified in diverse autotrophic bacteria and archaea, it is common in the biochemistry literature for the reductive mechanism to be inferred as the “direct reverse” of the oxidative mechanism by the ”principal of microreversibility.”[15] In the process of reducing carbon dioxide, the enzyme's C-cluster must first be activated from an oxidized to a reduced state before the Ni-CO2 bond is formed.[16]

Biological function

Carbon monoxide dehydrogenase participates in diverse prokaryotic biochemical pathways, including the metabolism of methanogenic, aerobic carboxidotrophic, acetogenic bacteria, sulfate-reducing, and hydrogenogenic bacteria.[1] The bidirectional reaction catalyzed by CODH plays a role in the carbon cycle allowing organisms to both make use of CO as a source of energy and utilize CO2 as a source of carbon. CODH can form a monofunctional enzyme, as is the case in Rhodospirillum rubram, or can form a cluster with acetyl-CoA synthase as has been shown in M.thermoacetica. When acting in concert, either as structurally independent enzymes or in a bifunctional CODH/ACS unit, the two catalytic sites are key to carbon fixation in the reductive acetyl-CoA pathway.[17]

Environmental relevance

CODH is important for maintaining current atmospheric conditions. Microbial metabolism of CO maintains ambient CO at levels safe for other forms of life.[18]

References

Further reading

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and USA.gov, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for USA.gov and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
 
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
 
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.
 


Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.