Surprising cofactors in metalloenzymes
Abstract
Transition metal complexes are located at the active sites of a number of enzymes involved in intriguing biochemical reactions. These complexes can exhibit a wide variety of chemical reactivity due to the ease at which transition metals can adopt different coordination environments and oxidation states. Crystallography has been a powerful technique for examining the structure and conformational variability of complex biological metallocenters. In particular, the past ten years have provided a wealth of structural information and several surprises concerning the metallocenters at the active sites of nitrogenase, hydrogenase and carbon monoxide dehydrogenase/acetyl-coenzyme A synthase.
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The catalysis was provided by the transition metals and transition metal sulfides themselves of the hydrothermal mound.
“The catalysis was provided by the transition metals and transition metal sulfides themselves of the hydrothermal mound.”
From Early bioenergetic evolution (2013) · cites this paper as [50]
The catalysis in CODH/ACS is performed by transition metals Fe and Ni coordinated as sulfide clusters.
“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 [50]
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Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms
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Sousa, F. L., Thiergart, T., Landan, G., Nelson-Sathi, S., Pereira, I. A. C., Allen, J. F., Lane, N., & Martin, W. F. (2013) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0088 · Cited by 286 · see citing works
“known), that they are replete with FeS proteins [50,60]) as seen in figure 5, that they live in habitats hardly different from those on the early Earth [11,30], that their energy metabolism is centred around flavin-based electron bifurcation [143]—the soluble precursor of the Q-cycle—and that the energetic pillar of t…”
BackgroundElucidation of an iterative process of carbon-carbon bond formation of prebiotic significance
Loison, A., Dubant, S., Adam, P., & Albrecht, P. (2010) · Astrobiology · doi:10.1089/ast.2009.0441 · Cited by 26 · see citing works
- Authors
- Drennan, C.
- Affiliations
- Massachusetts Institute of Technology (US)
- Corresponding author
- Drennan, C
- ORCID
- Drennan, C
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2003-04
- Volume
- 13
- Issue
- 2
- Pages
- 220-226
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2087052747
- Cited by
- 72
- References
- 1
- Citations by year
- 2026: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 1 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 2 · 2015: 4 · 2014: 2 · 2013: 4 · 2012: 1
- FWCI
- 6.27
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (GM 65337, R01GM065337)
- 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 › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- metalloenzymes, cofactors, transition metal complexes, active site, nitrogenase, hydrogenase, carbon monoxide dehydrogenase, coordination environment, oxidation state, conformational heterogeneity
- MeSH terms
- Aldehyde Oxidoreductases, Binding Sites, Coenzymes, Crystallography, Enzyme Activation, Hydrogenase, Iron, Metals, Models, Molecular, Multienzyme Complexes, Nickel, Nitrogenase, Protein Binding, Protein Conformation, Substrate Specificity, Transition Elements
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