In Vivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases.

ABSTRACT: EPR spectroscopy reveals the formation of two different semi-synthetic hydrogenases in vivo. [FeFe] hydrogenases are metalloenzymes that catalyze the interconversion of molecular hydrogen and protons. The reaction is catalyzed by the H-cluster, consisting of a canonical iron-sulfur cluster and an organometallic [2Fe] subsite. It was recently shown that the enzyme can be reconstituted with synthetic cofactors mimicking the composition of the [2Fe] subsite, resulting in semi-synthetic hydrogenases. Herein, we employ EPR spectroscopy to monitor the formation of two such semi-synthetic enzymes in whole cells. The study provides the first spectroscopic characterization of semi-synthetic hydrogenases in vivo, and the observation of two different oxidized states of the H-cluster under intracellul

SUBMITTER: Meszaros LS 

PROVIDER: S-EPMC6282530 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature