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Observation of the Fe-CN and Fe-CO vibrations in the active site of [NiFe] hydrogenase by nuclear resonance vibrational spectroscopy.

ABSTRACT: Nuclear inelastic scattering of (57)Fe labeled [NiFe] hydrogenase is shown to give information on different states of the enzyme. It was thus possible to detect and assign Fe-CO and Fe-CN bending and stretching vibrations of the active site outside the spectral range of the Fe-S cluster normal modes.

SUBMITTER: Kamali S

PROVIDER: S-EPMC3535562 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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Observation of the Fe-CN and Fe-CO vibrations in the active site of [NiFe] hydrogenase by nuclear resonance vibrational spectroscopy.

Kamali Saeed S Wang Hongxin H Mitra Devrani D Ogata Hideaki H Lubitz Wolfgang W Manor Brian C BC Rauchfuss Thomas B TB Byrne Deborah D Bonnefoy Violaine V Jenney Francis E FE Adams Michael W W MW Adams Michael W W MW Yoda Yoshitaka Y Alp Ercan E Zhao Jiyong J Cramer Stephen P SP

Angewandte Chemie (International ed. in English) 20121108 2

Nuclear inelastic scattering of (57)Fe labeled [NiFe] hydrogenase is shown to give information on different states of the enzyme. It was thus possible to detect and assign Fe-CO and Fe-CN bending and stretching vibrations of the active site outside the spectral range of the Fe-S cluster normal modes. ...[more]

PMID: 23136119

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Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy.

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