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Cited by 68Metalloenzymes and iron-sulfur proteinsCO2 Reduction Techniques and CatalystsMetal-Catalyzed Oxygenation Mechanisms

Metal centers in the anaerobic microbial metabolism of CO and CO2

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Bender, Güneş, Pierce, Elizabeth, Hill, Jeffrey A., Darty, Joseph E., Ragsdale, Stephen W.·2011·Metallomics
DOI 10.1039/c1mt00042jPMC PMC3964926
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Abstract

Carbon dioxide and carbon monoxide are important components of the carbon cycle. Major research efforts are underway to develop better technologies to utilize the abundant greenhouse gas, CO(2), for harnessing 'green' energy and producing biofuels. One strategy is to convert CO(2) into CO, which has been valued for many years as a synthetic feedstock for major industrial processes. Living organisms are masters of CO(2) and CO chemistry and, here, we review the elegant ways that metalloenzymes catalyze reactions involving these simple compounds. After describing the chemical and physical properties of CO and CO(2), we shift focus to the enzymes and the metal clusters in their active sites that catalyze transformations of these two molecules. We cover how the metal centers on CO dehydrogenase catalyze the interconversion of CO and CO(2) and how pyruvate oxidoreductase, which contains thiamin pyrophosphate and multiple Fe(4)S(4) clusters, catalyzes the addition and elimination of CO(2) during intermediary metabolism. We also describe how the nickel center at the active site of acetyl-CoA synthase utilizes CO to generate the central metabolite, acetyl-CoA, as part of the Wood-Ljungdahl pathway, and how CO is channelled from the CO dehydrogenase to the acetyl-CoA synthase active site. We cover how the corrinoid iron-sulfur protein interacts with acetyl-CoA synthase. This protein uses vitamin B(12) and a Fe(4)S(4) cluster to catalyze a key methyltransferase reaction involving an organometallic methyl-Co(3+) intermediate. Studies of CO and CO(2) enzymology are of practical significance, and offer fundamental insights into important biochemical reactions involving metallocenters that act as nucleophiles to form organometallic intermediates and catalyze C-C and C-S bond formations.

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  • FeS and FeNiS centres are particularly common in H2-oxidizing and CO2-reducing proteins of anaerobic prokaryotes.

    “Importantly, such FeS and FeNiS centres are particularly common in H2-oxidizing and CO2-reducing proteins of anaerobic prokaryotes [60].”

    From Early bioenergetic evolution (2013) · cites this paper as [60]

    Section V (page not provided) describes Fe–S clusters in CO2-reducing formate dehydrogenases and nickel–iron–sulfur centers in anaerobic CODHs that can reduce CO2. It does not establish that these centers are particularly common in H2-oxidizing proteins of anaerobic prokaryotes; its hydrogenase example concerns H2 formation instead. (LLM, conf=0.84)

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  • Reducing conditions of hydrothermal vents make energetics work in favour of amino acid and peptide synthesis, so an alkaline hydrothermal vent would, in principle, be working in the right direction thermodynamically.

    “Keeping in mind that the pyruvate-synthesizing enzyme of acetogens and methanogens, pyruvate synthase, is replete with FeS centres and uses acetyl-CoA, reduced Fd (Fdred) and CO2 as substrates [60], and also that reducing conditions of hydrothermal vents make energetics work in favour of amino acid and peptide synthesis [14], an alkaline hydrothermal vent would, in principle, be working in the”

    From Early bioenergetic evolution (2013) · cites this paper as [60]

    The sections on CO oxidation and PFOR discuss energy conservation and pyruvate synthesis, but do not address whether reducing conditions at hydrothermal vents favor amino acid or peptide synthesis. Searches for hydrothermal vents, peptides, and amino-acid synthesis found no passage establishing the claimed thermodynamic point. In the printed sentence, that point is attached to [14], while this paper appears to be cited for the separate pyruvate-synthase clause [60]. (LLM, conf=0.75)

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Authors
Bender, G., Pierce, E., Hill, J. A., Darty, J. E., & Ragsdale, S. W.
Affiliations
University of Michigan (US)
Corresponding author
Ragsdale, Stephen W.
ORCID
Venue
Metallomics
Publisher
Oxford University Press (OUP)
Published
2011
Volume
3
Issue
8
Pages
797
ISSN
  • 1756-5901 (ISSN-L)
  • 1756-591X
DOI
10.1039/c1mt00042j
PMC
PMC3964926
OpenAlex
W2102055688
Cited by
68
References
2
Citations by year
2026: 3 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 7 · 2021: 3 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 8 · 2016: 8 · 2015: 3 · 2014: 9 · 2013: 6 · 2012: 5
FWCI
0.34
Type
journal article
Language
en
Open access
Locations
  • Metallomics (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of General Medical Sciences (R37GM039451)
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › CO2 Reduction Techniques and Catalysts
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
metalloenzymes, carbon monoxide, carbon dioxide, CO dehydrogenase, thiamine pyrophosphate, Fe4S4 cluster, acetyl-CoA synthase, Wood-Ljungdahl pathway, vitamin B12, methyltransferase, anaerobic metabolism, metal clusters, CO2 utilization
MeSH terms
Anaerobiosis, Bacteria, Carbon Dioxide, Carbon Monoxide, Enzymes, Metals

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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