How Nitrogenase Shakes − Initial Information about P−Cluster and FeMo-cofactor Normal Modes from Nuclear Resonance Vibrational Spectroscopy (NRVS)
- 20 May 2006
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 128 (23), 7608-7612
- https://doi.org/10.1021/ja0603655
Abstract
Nitrogenase catalyzes a reaction critical for life, the reduction of N2 to 2NH3, yet we still know relatively little about its catalytic mechanism. We have used the synchrotron technique of 57Fe nuclear resonance vibrational spectroscopy (NRVS) to study the dynamics of the Fe−S clusters in this enzyme. The catalytic site FeMo-cofactor exhibits a strong signal near 190 cm-1, where conventional Fe−S clusters have weak NRVS. This intensity is ascribed to cluster breathing modes whose frequency is raised by an interstitial atom. A variety of Fe−S stretching modes are also observed between 250 and 400 cm-1. This work is the first spectroscopic information about the vibrational modes of the intact nitrogenase FeMo-cofactor and P-cluster.Keywords
This publication has 38 references indexed in Scilit:
- Towards an Understanding of the Workings of Nitrogenase from DFT CalculationsChemphyschem, 2005
- The Interstitial Atom of the Nitrogenase FeMo-Cofactor: ENDOR and ESEEM Evidence That it is Not a NitrogenJournal of the American Chemical Society, 2005
- The Hydrogen Chemistry of the FeMo-co Active Site of NitrogenaseJournal of the American Chemical Society, 2005
- The Mechanism of Nitrogenase. Computed Details of the Site and Geometry of Binding of Alkyne and Alkene Substrates and IntermediatesJournal of the American Chemical Society, 2004
- Chemical Activity of the Nitrogenase FeMo Cofactor with a Central Nitrogen Ligand: Density Functional StudyJournal of the American Chemical Society, 2004
- Nitrogen Binding to the FeMo-Cofactor of NitrogenaseJournal of the American Chemical Society, 2003
- The Interstitial Atom of the Nitrogenase FeMo-Cofactor: ENDOR and ESEEM Show It Is Not an Exchangeable NitrogenJournal of the American Chemical Society, 2003
- FeMo Cofactor of Nitrogenase: A Density Functional Study of States MN, MOX, MR, and MIJournal of the American Chemical Society, 2001
- Role of the MoFe Protein .alpha.-Subunit Histidine-195 Residue in FeMo-cofactor Binding and Nitrogenase CatalysisBiochemistry, 1995
- Resonance Raman Spectroscopy of Iron(III) Tetrathiolate Complexes: Implications for the Conformation and Force Field of RubredoxinJournal of the American Chemical Society, 1994