Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Arginine 95 is important for recruiting superoxide to the active site of the FerB flavoenzyme of Paracoccus denitrificans
Original language 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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10600 - Biological sciences
Result continuities
Project
<a href="/en/project/GA16-18476S" target="_blank" >GA16-18476S: Oxidative stress in denitrifying bacteria: deciphering functions of involved proteins and possible environmental impacts</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEBS Letters
ISSN
0014-5793
e-ISSN
1873-3468
Volume of the periodical
593
Issue of the periodical within the volume
7
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
697-702
UT code for WoS article
000465026200005
EID of the result in the Scopus database
2-s2.0-85063358061