Stepwise conversion of the Cys₆[4Fe-3S] to a Cys₄[4Fe-4S] cluster and its impact on the oxygen tolerance of [NiFe]-hydrogenase.

ABSTRACT: The membrane-bound [NiFe]-hydrogenase of Cupriavidus necator is a rare example of a truly O₂-tolerant hydrogenase. It catalyzes the oxidation of H₂ into 2e^- and 2H⁺ in the presence of high O₂ concentrations. This characteristic trait is intimately linked to the unique Cys₆[4Fe-3S] cluster located in the proximal position to the catalytic center and coordinated by six cysteine residues. Two of these cysteines play an essential role in redox-dependent cluster plasticity, which bestows the cofactor with the capacity to mediate two redox transitions at physiological potentials. Here, we investigated the individual roles of the two additional cysteines by replacing them individually as well as simultaneously with glycine.

SUBMITTER: Schmidt A 

PROVIDER: S-EPMC10583674 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature