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

SEDLÁČEK, Vojtěch and Igor KUČERA. Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans. FEBS Letters. Hoboken: Wiley, 2019, vol. 593, No 7, p. 697-702. ISSN 0014-5793. Available from: https://dx.doi.org/10.1002/1873-3468.13359.

Basic information

• Original name: Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans
• Authors: SEDLÁČEK, Vojtěch (203 Czech Republic, belonging to the institution) and Igor KUČERA (203 Czech Republic, guarantor, belonging to the institution).
• Edition: FEBS Letters, Hoboken, Wiley, 2019, 0014-5793.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• WWW: Full Text
• Impact factor: Impact factor: 3.057
• RIV identification code: RIV/00216224:14310/19:00107510
• Organization unit: Faculty of Science
• Doi: http://dx.doi.org/10.1002/1873-3468.13359
• UT WoS: 000465026200005
• Keywords in English: flavoprotein; antioxidant enzyme; chromate reductase; superoxide reductase
• Tags: rivok
• Tags: International impact, Reviewed

Abstract

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.

Links

• GA16-18476S, research and development project: Name: Oxidační stres u denitrifikačních baktérií: objasnění funkce zúčastněných proteinů a možných dopadů na životní prostředí

Investor: Czech Science Foundation