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A kinetic and thermodynamic understanding of O2 tolerance in [NiFe]-hydrogenases.

Abstract:

In biology, rapid oxidation and evolution of H(2) is catalyzed by metalloenzymes known as hydrogenases. These enzymes have unusual active sites, consisting of iron complexed by carbonyl, cyanide, and thiolate ligands, often together with nickel, and are typically inhibited or irreversibly damaged by O(2). The Knallgas bacterium Ralstonia eutropha H16 (Re) uses H(2) as an energy source with O(2) as a terminal electron acceptor, and its membrane-bound uptake [NiFe]-hydrogenase (MBH) is an impor...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.0905959106

Authors


Cracknell, JA More by this author
Friedrich, B More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
106
Issue:
49
Pages:
20681-20686
Publication date:
2009-12-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:98a61ee0-b6aa-42e3-b37f-8b3da3dde92d
Source identifiers:
34987
Local pid:
pubs:34987

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