Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site.

ABSTRACT: Elucidating the distribution of intermediates at the active site of redox metalloenzymes is vital to understanding their highly efficient catalysis. Here we demonstrate that it is possible to generate, and detect, the key catalytic redox states of an [FeFe]-hydrogenase in a protein crystal. Individual crystals of the prototypical [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI) are maintained under electrochemical control, allowing for precise tuning of the redox potential, while the crystal is simultaneously probed via Fourier Transform Infrared (FTIR) microspectroscopy. The high signal/noise spectra reveal potential-dependent variation in the distribution of redox states at the active site (H-cluster) according to state-specific vibrational bands from the endogeneou

SUBMITTER: Morra S 

PROVIDER: S-EPMC8453692 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature