Cited by 400Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsEnzyme Structure and Function

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Nickel-based Enzyme Systems

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Ragsdale, Stephen W.·2009·Journal of Biological Chemistry

DOI 10.1074/jbc.r900020200PMC PMC2707248

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Abstract

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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FIGURE 1. Structure of the NiFe active site and mechanism of hydrogenase. The structure is based on Protein Data Bank code 1CC1 (50). The mechanism of hydrogenase activation and catalysis is based on the work of Lill and Siegbahn (28). The asterisks indicate an EPR-active state.CC BY-NC · PubMed Central

FIGURE 2. Structure of F430 at the MCR active site and mechanism of methane formation. The structure is derived from Protein Data Bank code 1HBN (46). The bound CoM was omitted from the structure to focus on the tetrapyrrole.CC BY-NC · PubMed Central

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Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
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Kadish, K. M., Smith, K. M., & Guilard, R. (2003) · Elsevier eBooks · doi:10.1016/c2009-0-22714-0 · Cited by 2,594
Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
Zelko, I. N., Mariani, T. J., & Folz, R. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00905-x · Cited by 2,212
Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
Vignais, P. M., & Billoud, B. (2007) · Chemical Reviews · doi:10.1021/cr050196r · Cited by 1,617
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Ragsdale, S. W., & Pierce, E. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.08.012 · Cited by 1,409
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Nickel essentiality, toxicity, and carcinogenicity
Denkhaus, E., & Salnikow, K. (2002) · Critical Reviews in Oncology/Hematology · doi:10.1016/s1040-8428(01)00214-1 · Cited by 1,134
Jack bean urease (EC 3.5.1.5). Metalloenzyme. Simple biological role for nickel
Dixon, N. E., Gazzola, C., Blakeley, R. L., & Zerner, B. (1975) · Journal of the American Chemical Society · doi:10.1021/ja00847a045 · Cited by 833
On the origin of biochemistry at an alkaline hydrothermal vent
Martin, W., & Russell, M. J. (2007) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2006.1881 · Cited by 771
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Moore, G. R. (2002) · Journal of Organometallic Chemistry · doi:10.1016/s0022-328x(02)01715-1 · Cited by 701
Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation
Ermler, U., Grabarse, W., Shima, S., Goubeaud, M., & Thauer, R. K. (1997) · Science · doi:10.1126/science.278.5342.1457 · Cited by 615

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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)
DOI: 10.1074/jbc.r900020200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4138 d)
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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