Journal
EUROPEAN JOURNAL OF INORGANIC CHEMISTRY
Volume -, Issue 7, Pages 994-1004Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/ejic.201001148
Keywords
Hydrogenases; Biomimetics; Iron; Nickel; Oxygen; Sulfur
Categories
Funding
- National Science Foundation [CHE-0910679]
- R. A. Welch Foundation [A-0924]
- Freistaat Thuringen
- Studienstiftung des deutschen Volkes
- Japanese Society for the Promotion of Science (JSPS)
- Deutscher Akademischer Austauschdienst (DAAD)
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0910679] Funding Source: National Science Foundation
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The organometallic active sites in [NiFe]- and [FeFe]H(2)ases are sensitive to oxygen in varying degrees. The microorganisms that utilize these enzymes for their hydrogen metabolism, and the enzymes themselves, have evolved from a reducing to an oxidizing environment in ways to avoid competition with oxygen, primarily by burying the active site machinery deeply within the protein matrix. In the case of [NiFe]H(2)ase, biological studies indicate that repair mechanisms exist for reversible O-2-inhibition processes. This Microreview explores the possibility that S-oxygenation may represent reparable O-damaged enzyme active sites. Such S-oxygenation has precedent in chemical models for the terminal thiolate sulfur atoms of the nickel site in [NiFe]H(2)ase as well as the bridging thiolate sulfur in the [FeFe]H(2)ase active site. A discussion of the processes of O-2 damage leading to both reversible and irreversible enzyme inhibition, and reclamation of activity in the H(2)ases, as explored by various biochemical assays and spectroscopic methods, is also presented.
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