Structural Insight into Catalysis by the Flavin-Dependent NADH Oxidase (Pden_5119) 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%2F23%3A00130493" target="_blank" >RIV/00216224:14310/23:00130493 - isvavai.cz</a>
Result on the web
<a href="https://www.mdpi.com/1422-0067/24/4/3732" target="_blank" >https://www.mdpi.com/1422-0067/24/4/3732</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms24043732" target="_blank" >10.3390/ijms24043732</a>
Alternative languages
Result language
angličtina
Original language name
Structural Insight into Catalysis by the Flavin-Dependent NADH Oxidase (Pden_5119) of Paracoccus denitrificans
Original language description
The Pden_5119 protein oxidizes NADH with oxygen under mediation by the bound flavin mononucleotide (FMN) and may be involved in the maintenance of the cellular redox pool. In biochemical characterization, the curve of the pH-rate dependence was bell-shaped with pK(a1) = 6.6 and pK(a2) = 9.2 at 2 mu M FMN while it contained only a descending limb pK(a) of 9.7 at 50 mu M FMN. The enzyme was found to undergo inactivation by reagents reactive with histidine, lysine, tyrosine, and arginine. In the first three cases, FMN exerted a protective effect against the inactivation. X-ray structural analysis coupled with site-directed mutagenesis identified three amino acid residues important to the catalysis. Structural and kinetic data suggest that His-117 plays a role in the binding and positioning of the isoalloxazine ring of FMN, Lys-82 fixes the nicotinamide ring of NADH to support the proS-hydride transfer, and Arg-116 with its positive charge promotes the reaction between dioxygen and reduced flavin.
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
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Molecular Sciences
ISSN
1422-0067
e-ISSN
1422-0067
Volume of the periodical
24
Issue of the periodical within the volume
4
Country of publishing house
CH - SWITZERLAND
Number of pages
17
Pages from-to
1-17
UT code for WoS article
000945013900001
EID of the result in the Scopus database
2-s2.0-85149017927