Observation of the Fe[BOND]CN and Fe[BOND]CO Vibrations in the Active Site of [NiFe] Hydrogenase by Nuclear Resonance Vibrational Spectroscopy

Authors


  • This work was funded by the National Institutes of Health GM-65440 (S.P.C.) and GM-061153 (T.B.R.), the DOE Office of Biological and Environmental Research (S.P.C.), BMBF (03SF0355C), EU/Energy Network project SOLAR-H2 (FP7 contract 212508), and Max Planck Society (W.L. and H.O.). A.P.S. is supported by the DOE Office of Basic Energy Sciences. The proposal number in SPring-8 is 2010B0032-2012 A0032.

Abstract

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

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