The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal.

ABSTRACT: [FeFe]-hydrogenases catalyze the reversible conversion of molecular hydrogen into protons and electrons with remarkable efficiency. However, their industrial applications are limited by their oxygen sensitivity. Recently, it was shown that the [FeFe]-hydrogenase from Clostridium beijerinckii (CbA5H) is oxygen-resistant and can be reactivated after oxygen exposure. In this work, we used multifrequency continuous wave and pulsed electron paramagnetic resonance (EPR) spectroscopy to characterize the active center of CbA5H, the H-cluster. Under oxidizing conditions, the spectra were dominated by an additional and unprecedented radical species. The generation of this radical signal depends on the presence of an intact H-cluster and a complete proton transfer pathway including the bridgin

SUBMITTER: Heghmanns M 

PROVIDER: S-EPMC9214887 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature