Nuclear Resonance Vibrational Spectroscopy (NRVS) is a powerful and relatively new way to study Fe in biological systems. In this synchrotron radiation technique, a sample is excited with a ~1 meV bandwidth beam near the Mössbauer resonance, and the delayed fluorescence is recorded as a function of excitation energy. When applied to Fe-containing samples, NRVS is sensitive only to vibrations involving motion of the 57Fe nucleus. Hydrogenases (H2ases) are the enzymes responsible for interconversion of protons and electrons with molecular dihydrogen. It has recently been shown that a candidate hydride species can be produced by disruption of the proton transport chain, either through amino acid substitutions or though changes in the aminodithiolate ligand. In this talk I will describe the NRVS approach that we have used to define Fe-H interactions in [FeFe] H2ase, including identification of enzyme intermediates.

Nuclear Resonance Vibrational Spectroscopy (NRVS) of FeFe hydrogenase: New evidence of enzyme intermediates

253rd National Meeting (2017)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.