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Cited by 116Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsOrganometallic Complex Synthesis and Catalysis

Metal–metal bonds in biology

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Lindahl, Paul A.·2012·Journal of Inorganic Biochemistry
DOI 10.1016/j.jinorgbio.2011.08.012PMC PMC3232296
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Abstract

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 O(2)-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 CO(2) 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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  • Enzymes of core carbon and energy pathways in modern anaerobic autotrophs are replete with FeS, FeNiS and MoS (WS) centres.

    “This is an important similarity to modern anaerobic autotrophs, whose enzymes of core carbon and energy pathways are replete with FeS, FeNiS and MoS (WS) centres, FeS and NiS usually being incorporated into proteins via cysteine residues [54–58], Mo and W usually being complexed by thiols of the molybdopterin cofactor MoCo [59].”

    From Early bioenergetic evolution (2013) · cites this paper as [57]

    The Introduction (§1.1; page unavailable) describes Fe–S and Ni–Fe–S clusters in enzymes found in anaerobic bacteria and archaea, including hydrogenases, carbon monoxide dehydrogenases, and acetyl-CoA synthases. It does not establish that core-pathway enzymes in anaerobic autotrophs generally are replete with these centres, and it does not describe Mo–S or W–S centres. (LLM, conf=0.87)

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Authors
Lindahl, P. A.
Affiliations
Texas A&M University (US)
Corresponding author
Lindahl, Paul A.
ORCID
Lindahl, Paul A.
Venue
Journal of Inorganic Biochemistry
Publisher
Elsevier BV
Published
2012-01
Volume
106
Issue
1
Pages
172-178
ISSN
0162-0134 (ISSN-L)
DOI
10.1016/j.jinorgbio.2011.08.012
PMC
PMC3232296
OpenAlex
W2145024056
Cited by
116
References
1
Citations by year
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FWCI
0.53
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Journal of Inorganic Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of General Medical Sciences (R01GM046441, R56GM046441, GM 46441)
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Physical Sciences › Chemistry › Organic Chemistry › Organometallic Complex Synthesis and Catalysis
Keywords
metal-metal bonding, metalloenzymes, carbon monoxide dehydrogenase, acetyl-CoA synthase, [NiFe] hydrogenase, reductive activation, oxidative addition, redox potential, sulfur-containing ligands, Fe-Fe bond, multi-electron redox
MeSH terms
Acetate-CoA Ligase, Aldehyde Oxidoreductases, Hydrogenase, Iron, Metalloproteins, Models, Molecular, Multienzyme Complexes, Nickel, Protein Binding, Protein Conformation

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