Acetyl‐coenzyme A Synthases and Nickel‐Containing Carbon Monoxide Dehydrogenases

Lindahl, Paul A.; Graham, David E.

doi:10.1002/9780470028131.ch9

Cited by 22 publications

(29 citation statements)

References 80 publications

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“…However, many mechanistic details of acetyl-CoA formation by ACS have not yet been elucidated. The active A-cluster has been characterized as a Ni 2 Fe 4 S 4 center in the crystal structures of both bi-functional CODH/ACS Mot and mono-functional ACS Ch (5,9), in agreement with many previous studies, as reviewed in (10,11). Catalysis involves three substrates, CoA, CO and the cobalt-containing methyl-carrying corrinoid iron-sulfur protein (CoFeSP):

CoA - {normalS}^{-} + CO + {CH}_{3}^{-} - Co (III) FeSP ⇄ CoA - SC (normalO) {CH}_{3} + Co (normalI) FeSP .

…”

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confidence: 87%

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Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase from Moorella thermoacetica^,

et al. 2009

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Ni-dependent Acetyl-CoA synthase (ACS) and CO dehydrogenase (CODH) constitute the central enzyme complex of the Wood-Ljungdahl pathway of acetyl-CoA formation. The crystal structure of a recombinant bacterial ACS lacking the N-terminal domain that interacts with CODH shows a large reorganization of the remaining two globular domains, producing a narrow cleft of suitable size, shape and nature to bind CoA. Sequence comparisons with homologous archaeal enzymes that naturally lack the N-terminal domain show that many amino acids lining this cleft are conserved. Besides the typical [4Fe-4S] center, the A-cluster contains only one proximal metal ion that, according to anomalous scattering data, is most likely Cu or Zn. Incorporation of a functional Ni 2 Fe 4 S 4 A-cluster would require only minor structural rearrangements. Using available structures, a plausible model of the interaction between CODH and the smaller ACS in archaeal multi-enzyme complexes is presented, along with a discussion of evolutionary relationships of the archaeal and bacterial enzymes.Ni-dependent acetyl coenzyme A synthase (ACS) is a NiFeS-cluster enzyme that requires strict anoxic conditions to function. In the acetogenic bacterium Moorella thermoacetica (Mot), the ACS α-subunit forms an α 2 β 2 heterotetramer with the Ni-containing carbon monoxide dehydrogenase (CODH) β-subunit (1). This association constitutes the central enzyme complex of the anaerobic Wood-Ljungdahl pathway of acetyl-CoA synthesis from CO 2 (2,3). The structure of this complex is known in two crystal forms (4,5) and shows a long hydrophobic tunnel network that allows the CO produced at the CODH active site, the C-cluster, to be used at the ACS active site, the A-cluster, without being released to the medium. Our understanding of CO 2 reduction to CO by CODH has progressed significantly thanks to the recent crystal structures of key catalytic intermediates in the homodimeric β 2 enzyme from † This study was supported by institutional funding from the CEA and the CNRS and by the National Institute of Health (GM046441 PAL). ‡ The atomic coordinates and structure factors (accession number 3GIT) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics (http://www.pdb.org).*To whom correspondence should be addressed. AV: Tel. +33438789606, Fax +33438785122, E-mail anne.volbeda@ibs.fr; JCFC: Tel. +33438785920, Fax +33438785122, E-mail juan.fontecilla@ibs.fr.. # Current address: Department of Chemistry, Institute of Biomedical Sciences, Fudan University, Shanghai, 200043, P.R. China Supporting Information Available. Superposition statistics of bacterial CODH/ACS and archaeal CODH, sequence alignment of bacterial ACS with archaeal CODH and structure comparison of CODH and HCP. This material is available free of charge via the Internet at http://pubs.acs.org. NIH Public Access Author ManuscriptBiochemistry. Author manuscript; available in PMC 2010 August 25. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author ManuscriptC...

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CoA - {normalS}^{-} + CO + {CH}_{3}^{-} - Co (III) FeSP ⇄ CoA - SC (normalO) {CH}_{3} + Co (normalI) FeSP .

…”

supporting

confidence: 87%

“…Therefore, the high degree of residue conservation at the A2 / A3 interface suggests a functional role for the α 49(T) conformation. The invariant residues in Figure 6 are also highly conserved in an alignment of 7 bacterial and 13 archaeal ACS amino acid sequences (10). …”

Section: Resultsmentioning

confidence: 99%

Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase from Moorella thermoacetica^,

et al. 2009

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“…The enzyme activates CO toward reaction with a methyl group (donated by the corrinoid iron–sulfur protein, CFeSP) and coenzyme A to generate acetyl-CoA, which serves as a source of energy and cell carbon for various anaerobic microbes. 140 The stoichiometries of the carbonylation using CO (involving only ACS) or CO 2 (requiring both CODH and ACS) are shown in eqs 19 and 20.…”

Section: C–c Bond-forming Reactions Involving Co and Co2mentioning

confidence: 99%

Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO₂ Fixation

et al. 2013

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“…Numerous model complexes of the H-cluster have been synthesized, most of which are based on an Fe 2 (dithiolate) core that forms an Fe-Fe bond under reducing and non-protonated conditions [1]. The exact site of protonation is uncertain but a terminal site is kinetically favored, followed by rearrangement to the bridging position.…”

Section: 4 Evidence For M-m Bonds In Metalloenzymesmentioning

confidence: 99%

“…Nickel-containing carbon monoxide dehydrogenases (CODHs [1]), acetyl-CoA synthases (ACSs [2]), diiron hydrogenases ([FeFe] Hases [3]) and nickel-and-iron hydrogenases ([NiFe] Hases [4]) are distinct, genetically unrelated, metalloenzymes, yet they share a remarkable number of structural and functional properties. When these properties are viewed collectively, a pattern emerges that suggests the formation of metal-metal (M-M) bonds during catalysis and the functional importance of such bonds.…”

Section: 1 Introductionmentioning

confidence: 99%

Metal–metal bonds in biology

Lindahl

2012

Journal of Inorganic Biochemistry

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Nickel-containing carbon monoxide dehydrogenases, acetyl-CoA synthases, nickel-iron hydrogenases, and diron hydrogenases are distinct metalloenzymes yet they share a number of important characteristics. All are O2-sensitive, with active-sites composed of iron and/or nickel ions coordinated primarily by sulfur ligands. In each case, two metals are juxtaposed at the “heart” of the active site, within range of forming metal-metal bonds. These active-site clusters exhibit multielectron redox abilities and must be reductively activated for catalysis. Reduction potentials are milder than expected based on formal oxidation state changes. When reductively activated, each cluster attacks an electrophilic substrate via an oxidative addition reaction. This affords a two-electron-reduced substrate bound to one or both metals of an oxidized cluster. M-M bonds have been established in hydrogenases where they serve to initiate the oxidative addition of protons and perhaps stabilize active sites in multiple redox states. The same may be true of the CODH and ACS active sites – Ni-Fe and Ni-Ni bonds in these sites may play critical roles in catalysis, stabilizing low-valence states and initiating oxidative addition of CO2 and methyl group cations, respectively. In this article, the structural and functional commonalities of these metalloenzyme active sites are described, and the case is made for the formation and use of metal-metal bonds in each enzyme mentioned. As a post-script, the importance of Fe-Fe bonds in the nitrogenase FeMoco active site is discussed.

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Acetyl‐coenzyme A Synthases and Nickel‐Containing Carbon Monoxide Dehydrogenases

Cited by 22 publications

References 80 publications

Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase from Moorella thermoacetica^,

Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase from Moorella thermoacetica^,

Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO₂ Fixation

Metal–metal bonds in biology

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Acetyl‐coenzyme A Synthases and Nickel‐Containing Carbon Monoxide Dehydrogenases

Cited by 22 publications

References 80 publications

Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase from Moorella thermoacetica,

Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase from Moorella thermoacetica,

Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO2 Fixation

Metal–metal bonds in biology

Contact Info

Product

Resources

About

Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase from Moorella thermoacetica^,

Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase from Moorella thermoacetica^,

Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO₂ Fixation