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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F19%3A00107510" target="_blank" >RIV/00216224:14310/19:00107510 - isvavai.cz</a>

Výsledek na webu

<a href="https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13359" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13359</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/1873-3468.13359" target="_blank" >10.1002/1873-3468.13359</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10600 - Biological sciences

Projekt

<a href="/cs/project/GA16-18476S" target="_blank" >GA16-18476S: Oxidační stres u denitrifikačních baktérií: objasnění funkce zúčastněných proteinů a možných dopadů na životní prostředí</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

FEBS Letters

ISSN

0014-5793

e-ISSN

1873-3468

Svazek periodika

593

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

6

Strana od-do

697-702

Kód UT WoS článku

000465026200005

EID výsledku v databázi Scopus

2-s2.0-85063358061