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Crystal structure of the O(2)-tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome b.

Abstract:

We report the 3.3 Å resolution structure of dimeric membrane-bound O(2)-tolerant hydrogenase 1 from Escherichia coli in a 2:1 complex with its physiological partner, cytochrome b. From the short distance between distal [Fe(4)S(4)] clusters, we predict rapid transfer of H(2)-derived electrons between hydrogenase heterodimers. Thus, under low O(2) levels, a functional active site in one heterodimer can reductively reactivate its O(2)-exposed counterpart in the other. Hydrogenase 1 is maximally ...

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Publication status:
Published

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Publisher copy:
10.1016/j.str.2012.11.010

Authors


Volbeda, A More by this author
Darnault, C More by this author
Sargent, F More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
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Journal:
Structure (London, England : 1993)
Volume:
21
Issue:
1
Pages:
184-190
Publication date:
2013-01-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:79599767-65e4-482c-8fa7-487f9d1553f0
Source identifiers:
379448
Local pid:
pubs:379448

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