The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster-Reference-Cited by-同舟云学术

The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster

Published:2014-03-16 Issue:4 Volume:6 Page:336-342
ISSN:1755-4330
Container-title:Nature Chemistry
language:en
Short-container-title:Nature Chem

Author:

Fourmond Vincent,Greco Claudio,Sybirna Kateryna,Baffert Carole,Wang Po-Hung,Ezanno Pierre,Montefiori Marco,Bruschi Maurizio,Meynial-Salles Isabelle,Soucaille Philippe,Blumberger Jochen,Bottin Hervé,De Gioia Luca,Léger Christophe

Publisher

Springer Science and Business Media LLC

Subject

General Chemical Engineering,General Chemistry

Link

http://www.nature.com/articles/nchem.1892.pdf

Reference50 articles.

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2. Tard, C. & Pickett, C. J. Structural and functional analogues of the active sites of the [Fe]-, [NiFe]-, and [FeFe]-hydrogenases. Chem. Rev. 109, 2245–2274 (2009).

3. Liu, T., Dubois, D. L. & Bullock, R. M. An iron complex with pendent amines as a molecular electrocatalyst for oxidation of hydrogen. Nature Chem. 5, 228–233 (2013).

4. Fontecilla-Camps, J. C., Volbeda, A., Cavazza, C. & Nicolet, Y. Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chem. Rev. 107, 4273–4303 (2007).

5. Hsieh, C-H. et al. Structural and spectroscopic features of mixed valent FeIIFeI complexes and factors related to the rotated configuration of diiron hydrogenase. J. Am. Chem. Soc. 134, 13089–13102 (2012).

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