How Nitrogenase Shakes − Initial Information about P−Cluster and FeMo-cofactor Normal Modes from Nuclear Resonance Vibrational Spectroscopy (NRVS)
Year: 2006
Type: article
Abstract: Nitrogenase catalyzes a reaction critical for life, the reduction of N(2) to 2NH(3), yet we still know relatively little about its catalytic mechanism. We have used the synchrotron technique of (57)Fe 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.
DOI: 10.1021/ja0603655
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: green
Awards: Electronic Structure of Iron-Sulfur and Related Proteins, MOFE PROTEIN PROSTHETIC GROUPS IN NITROGENASE CATALYSIS, SOFT X-RAY AND EXAFS SPECTROSCOPY OF METALLOPROTEINS, Soft X-Ray, XMCD, and EXAFS of Metalloproteins, Spectroscopy of Fe-S Cluster Proteins -- Information for Structure and Function
OpenAlex ID: W2051873806