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Nickel-based Enzyme Systems
Open accessAbstract
Of the eight known nickel enzymes, all but glyoxylase I catalyze the use and/or production of gases central to the global carbon, nitrogen, and oxygen cycles. Nickel appears to have been selected for its plasticity in coordination and redox chemistry and is able to cycle through three redox states (1+, 2+, 3+) and to catalyze reactions spanning approximately 1.5 V. This minireview focuses on the catalytic mechanisms of nickel enzymes, with an emphasis on the role(s) of the metal center. The metal centers vary from mononuclear to complex metal clusters and catalyze simple hydrolytic to multistep redox reactions.
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“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 [56]
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“In the enzymatic mechanism [56], electrons from a low-potential Fd are used by the enzyme to reduce one molecule of CO2 to CO at an FeNiS cluster called the C cluster; that CO migrates to a second FeNiS cluster in the enzyme (the A cluster), where it binds one of two Ni atoms at the Nip site to form a Ni-bound carbonyl group, where the two-electron donating property of Ni is important in the”
From Early bioenergetic evolution (2013) · cites this paper as [56]
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“The catalysis in CODH/ACS is performed by transition metals (Fe and Ni) coordinated as sulfide clusters [50,56,73].”
From Early bioenergetic evolution (2013) · cites this paper as [56]
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Citations
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Metadata
- Authors
- Ragsdale, S. W.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Ragsdale, Stephen W.
- ORCID
- Ragsdale, Stephen W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-07
- Volume
- 284
- Issue
- 28
- Pages
- 18571-18575
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2707248
- OpenAlex
- W1996983125
- Cited by
- 400
- References
- 40
- Citations by year
- 2026: 24 · 2025: 32 · 2024: 39 · 2023: 26 · 2022: 30 · 2021: 24 · 2020: 24 · 2019: 26 · 2018: 26 · 2017: 20 · 2016: 11 · 2015: 15 · 2014: 26 · 2013: 22 · 2012: 23
- FWCI
- 0.95
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM039451)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- nickel enzymes, nickel coordination chemistry, redox state, catalytic mechanism, metal centers, metal clusters, carbon cycle, nitrogen cycling, oxygen cycle, hydrolysis
- MeSH terms
- Acetate-CoA Ligase, Biochemistry, Carbon, Catalysis, Enzymes, Hydrogenase, Hydrolysis, Metals, Models, Molecular, Molecular Conformation, Nickel, Nitrogen, Oxidation-Reduction, Oxygen, Urease
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