Ontology highlight
ABSTRACT:
SUBMITTER: Xiao Y
PROVIDER: S-EPMC3174779 | biostudies-literature | 2006 Jun
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20060601 23
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 freq ...[more]