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          Institute: MPI für Biophysik     Collection: Abt. Molekulare Membranbiologie     Display Documents



  history
ID: 680384.0, MPI für Biophysik / Abt. Molekulare Membranbiologie
Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H2-Activation Site
Authors:Tamura, Haruka; Salomone-Stagni, Marco; Fujishiro, Takashi; Warkentin, Eberhard; Meyer-Klaucke, Wolfram; Ermler, Ulrich; Shima, Seigo
Language:English
Date of Publication (YYYY-MM-DD):2013-09-09
Title of Journal:Angwandte Chemie International Edition
Journal Abbrev.:Ang. Chem. Int. Ed.
Volume:52
Issue / Number:37
Start Page:9656
End Page:9659
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:Inhibition mechanism: Isocyanides strongly inhibit [Fe]-hydrogenase. X-ray crystallography and X-ray absorption spectroscopy revealed that the isocyanide binds to the trans position, versus the acyl carbon of the Fe center, and is covalently bound to the pyridinol hydroxy oxygen. These results also indicated that the hydroxy group is essential for H2 activation.
Free Keywords:Hydrogenases; iron-guanylylpyridinol cofactor; isocyanide ligands; X-ray absorption spectroscopy; X-ray diffraction
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Molekulare Membranbiologie
MPI für terrestrische Mikrobiologie/Department-independent groups
External Affiliations:EMBL Hamburg, Notkestrasse 85, 22603 Hamburg, Germany.
PRESTO Japan Science and Technology Agency (JST), Honcho, Kawaguchi, Saitama 332-0012, Japan;
University of Paderborn, Department of Chemistry, Warburger Strasse 100, 33098 Paderborn, Germany
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