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

Journal article

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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Authors: Volbeda, A; Darnault, C; Parkin, A; Sargent, F; Armstrong, F

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 21
• Issue: 1
• Pages: 184-190
• Publication date: 2013-01-01
• DOI: 10.1016/j.str.2012.11.010
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Protein Structure, Quaternary; Hydrophobic and Hydrophilic Interactions; Protein Binding; Escherichia coli; Heme; Crystallography, X-Ray; Hydrogenase; Catalytic Domain; Surface Properties; Protein Interaction Domains and Motifs; Models, Molecular; Protein Structure, Secondary; Escherichia coli Proteins