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

J 2019

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

SEDLÁČEK, Vojtěch a Igor KUČERA

Základní údaje

Originální název

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

Autoři

SEDLÁČEK, Vojtěch (203 Česká republika, domácí) a Igor KUČERA (203 Česká republika, garant, domácí)

Vydání

FEBS Letters, Hoboken, Wiley, 2019, 0014-5793

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Full Text

Impakt faktor

Impact factor: 3.057

Kód RIV

RIV/00216224:14310/19:00107510

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1002/1873-3468.13359

UT WoS

000465026200005

Klíčová slova anglicky

flavoprotein; antioxidant enzyme; chromate reductase; superoxide reductase

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 19. 3. 2020 15:46, Mgr. Marie Šípková, DiS.

Anotace

V originále

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.

Návaznosti

GA16-18476S, projekt VaV

Název: Oxidační stres u denitrifikačních baktérií: objasnění funkce zúčastněných proteinů a možných dopadů na životní prostředí

Investor: Grantová agentura ČR, Oxidační stres u denitrifikačních baktérií: objasnění funkce zúčastněných proteinů a možných dopadů na životní prostředí

Citovat

SEDLÁČEK, Vojtěch a 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, roč. 593, č. 7, s. 697-702. ISSN 0014-5793. Dostupné z: https://dx.doi.org/10.1002/1873-3468.13359.

@article{1545943,
   author = {Sedláček, Vojtěch and Kučera, Igor},
   article_location = {Hoboken},
   article_number = {7},
   doi = {http://dx.doi.org/10.1002/1873-3468.13359},
   keywords = {flavoprotein; antioxidant enzyme; chromate reductase; superoxide reductase},
   language = {eng},
   issn = {0014-5793},
   journal = {FEBS Letters},
   title = {Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans},
   url = {https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13359},
   volume = {593},
   year = {2019}
}

TY  - JOUR
ID  - 1545943
AU  - Sedláček, Vojtěch - Kučera, Igor
PY  - 2019
TI  - Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans
JF  - FEBS Letters
VL  - 593
IS  - 7
SP  - 697-702
EP  - 697-702
PB  - Wiley
SN  - 00145793
KW  - flavoprotein
KW  - antioxidant enzyme
KW  - chromate reductase
KW  - superoxide reductase
UR  - https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13359
L2  - https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13359
N2  - 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.
ER  -

SEDLÁČEK, Vojtěch a Igor KUČERA. Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans. \textit{FEBS Letters}. Hoboken: Wiley, 2019, roč.~593, č.~7, s.~697-702. ISSN~0014-5793. Dostupné z: https://dx.doi.org/10.1002/1873-3468.13359.

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