Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen--the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases.

Journal article

"Hyd-1", produced by Escherichia coli , exemplifies a special class of [NiFe]-hydrogenase that can sustain high catalytic H(2) oxidation activity in the presence of O(2)-an intruder that normally incapacitates the sulfur- and electron-rich active site. The mechanism of "O(2) tolerance" involves a critical role for the Fe-S clusters of the electron relay, which is to ensure the availability-for immediate transfer back to the active site-of all of the electrons required to reduce an attacking ...

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Authors: Evans, R; Parkin, A; Roessler, M; Murphy, B; Adamson, H

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 135
• Issue: 7
• Pages: 2694-2707
• Publication date: 2013-02-01
• DOI: 10.1021/ja311055d
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Genetic Variation; Oxidation-Reduction; Hydrogen; Crystallography, X-Ray; Sequence Alignment; Oxygen; Iron-Sulfur Proteins; Amino Acid Sequence; Molecular Sequence Data; Hydrogenase; Escherichia coli; Models, Biological