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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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