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- W1966467441 abstract "Recent research on hydrogenases has been notably motivated by a desire to utilize these remarkable hydrogen oxidation catalysts in biotechnological applications. Progress in the development of such applications is substantially hindered by the oxygen sensitivity of the majority of hydrogenases. This problem tends to inspire the study of organisms such as Ralstonia eutropha H16 that produce oxygen-tolerant [NiFe]-hydrogenases. R. eutropha H16 serves as an excellent model system in that it produces three distinct [NiFe]-hydrogenases that each serve unique physiological roles: a membrane-bound hydrogenase (MBH) coupled to the respiratory chain, a cytoplasmic, soluble hydrogenase (SH) able to generate reducing equivalents by reducing NAD+ at the expense of hydrogen, and a regulatory hydrogenase (RH) which acts in a signal transduction cascade to control hydrogenase gene transcription. This review will present recent results regarding the biosynthesis, regulation, structure, activity, and spectroscopy of these enzymes. This information will be discussed in light of the question how do organisms adapt the prototypical [NiFe]-hydrogenase system to function in the presence of oxygen." @default.
- W1966467441 created "2016-06-24" @default.
- W1966467441 creator A5006549777 @default.
- W1966467441 creator A5010927081 @default.
- W1966467441 creator A5026646011 @default.
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- W1966467441 creator A5072409509 @default.
- W1966467441 creator A5078374648 @default.
- W1966467441 creator A5080067298 @default.
- W1966467441 date "2005-01-01" @default.
- W1966467441 modified "2023-10-15" @default.
- W1966467441 title "[NiFe]-Hydrogenases of <i>Ralstonia eutropha</i> H16: Modular Enzymes for Oxygen-Tolerant Biological Hydrogen Oxidation" @default.
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