Single Crystal EPR Studies of the Reduced Active Site of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F-Reference-Cited by-同舟云学术

Single Crystal EPR Studies of the Reduced Active Site of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F

Published:2002-12-06 Issue:1 Volume:125 Page:83-93
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Foerster Stefanie¹,Stein Matthias¹,Brecht Marc¹,Ogata Hideaki¹,Higuchi Yoshiki¹,Lubitz Wolfgang¹

Affiliation:

1. Contribution from the Max-Volmer-Laboratorium für Biophysikalische Chemie, Fakultät für Mathematik und Naturwissenschaften, Technische Universität Berlin, D-10623 Berlin, Germany, Division of Chemistry, Graduate School of Science Kyoto University, Sakyo-Ku, Kyoto 606-1, Japan and Max-Planck-Institut für Strahlenchemie, P.O. Box 10 13 65, D-45413 Mülheim an der Ruhr, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja027522u

Reference70 articles.

1. Energy conservation in chemotrophic anaerobic bacteria

2. A novel very small subunit of a selenium containing [NiFe] hydrogenease of Methanococcus voltae is postranslationally processed by cleavage at a defined position

3. Reactions with Molecular Hydrogen in Microorganisms: Evidence for a Purely Organic Hydrogenation Catalyst

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