Publication details

Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans

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Year of publication 2019
Type Article in Periodical
Magazine / Source FEBS Letters
MU Faculty or unit

Faculty of Science

Web Full Text
Keywords flavoprotein; antioxidant enzyme; chromate reductase; superoxide reductase
Description Ferric reductase B (FerB) is a flavin mononucleotide (FMN)containing NAD(P)H:acceptor oxidoreductase structurally close to the Gluconacetobacter hansenii chromate reductase (ChrR). The crystal structure of ChrR was previously determined with a chloride bound proximal to FMN in the vicinity of Arg101, and the authors suggested that the anionic electron acceptors, chromate and uranyl tricarbonate, bind similarly. Here, we identify the corresponding arginine residue in FerB (Arg95) as being important for the reaction of FerB with superoxide. Four mutants at position 95 were prepared and found kinetically to have impaired capacity for superoxide binding. Stopped flow data for the flavin cofactor showed that the oxidative step is rate limiting for catalytic turnover. The findings are consistent with a role for FerB as a superoxide scavenging contributor.
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