Work

Cover Picture: Observation of the FeCN and FeCO Vibrations in the Active Site of [NiFe] Hydrogenase by Nuclear Resonance Vibrational Spectroscopy (Angew. Chem. Int. Ed. 2/2013)

Year: 2012

Type: article

Abstract: The active site of [NiFe] hydrogenase is an excellent catalyst for hydrogen conversion with an intriguing ability to recover from exposure to dioxygen. In their Communication on page 724 ff., W. Lubitz, S. P. Cramer, and co-workers use the synchrotron technique of nuclear resonance vibrational spectroscopy to identify normal modes associated with active-site FeCN and FeCO motion.

Source: Angewandte Chemie International Edition

DOI: 10.1002/anie.201208498

Authors: Saeed Kamali, Hongxin Wang, Devrani Mitra, Hideaki Ogata, Wolfgang Lubitz, Brian C. Manor, Thomas B. Rauchfuss, Deborah Byrne, Violaine Bonnefoy, Francis E. Jenney, Michael W. W. Adams, Yoshitaka Yoda, Ercan Alp, Jiyong Zhao, Stephen P. Cramer

Institutions: University of California, Davis, Lawrence Berkeley National Laboratory, Max Planck Institute for Chemical Energy Conversion, University of Illinois Urbana-Champaign, Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Centre National de la Recherche Scientifique, Laboratoire de Chimie Bactérienne, Philadelphia College of Osteopathic Medicine, University of Georgia, SPring-8, Japan Synchrotron Radiation Research Institute, Spring-8 (Japan), Argonne National Laboratory, Advanced Photon Source

Language: English

Topic: Metalloenzymes and iron-sulfur proteins

Subfield: Renewable Energy, Sustainability and the Environment

Field: Energy

Domain: Physical Sciences

Open Access status: bronze

OpenAlex ID: W2050017205

FWCI:

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