Spectroscopic and Structural Characterization of Reduced Desulfovibrio vulgaris Hildenborough W-FdhAB Reveals Stable Metal Coordination during Catalysis.

ABSTRACT: Metal-dependent formate dehydrogenases are important enzymes due to their activity of CO₂ reduction to formate. The tungsten-containing FdhAB formate dehydrogenase from Desulfovibrio vulgaris Hildenborough is a good example displaying high activity, simple composition, and a notable structural and catalytic robustness. Here, we report the first spectroscopic redox characterization of FdhAB metal centers by EPR. Titration with dithionite or formate leads to reduction of three [4Fe-4S]¹⁺ clusters, and full reduction requires Ti(III)-citrate. The redox potentials of the four [4Fe-4S]¹⁺ centers range between -250 and -530 mV. Two distinct W^V signals were detected, W_D^V and W_F^V, which differ in only th

SUBMITTER: Oliveira AR 

PROVIDER: S-EPMC9774666 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature