KRYL, Martin, Vojtěch SEDLÁČEK and Igor KUČERA. Structural Insight into Catalysis by the Flavin-Dependent NADH Oxidase (Pden_5119) of Paracoccus denitrificans. International Journal of Molecular Sciences. Basel: Multidisciplinary Digital Publishing Institute, 2023, vol. 24, No 4, p. 1-17. ISSN 1422-0067. Available from: https://dx.doi.org/10.3390/ijms24043732.
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Basic information
Original name Structural Insight into Catalysis by the Flavin-Dependent NADH Oxidase (Pden_5119) of Paracoccus denitrificans
Authors KRYL, Martin (203 Czech Republic, belonging to the institution), Vojtěch SEDLÁČEK (203 Czech Republic, belonging to the institution) and Igor KUČERA (203 Czech Republic, guarantor, belonging to the institution).
Edition International Journal of Molecular Sciences, Basel, Multidisciplinary Digital Publishing Institute, 2023, 1422-0067.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Switzerland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 5.600 in 2022
RIV identification code RIV/00216224:14310/23:00130493
Organization unit Faculty of Science
Doi http://dx.doi.org/10.3390/ijms24043732
UT WoS 000945013900001
Keywords in English FMN; NADH; dioxygen reduction; Paracoccus denitrificans
Tags rivok
Tags International impact, Reviewed
Changed by Changed by: prof. RNDr. Igor Kučera, DrSc., učo 911. Changed: 26/1/2024 07:46.
Abstract
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.
Links
EF18_046/0015974, research and development projectName: Modernizace České infrastruktury pro integrativní strukturní biologii
GA16-18476S, research and development projectName: Oxidační stres u denitrifikačních baktérií: objasnění funkce zúčastněných proteinů a možných dopadů na životní prostředí
Investor: Czech Science Foundation
LM2023042, research and development projectName: Česká infrastruktura pro integrativní strukturní biologii
Investor: Ministry of Education, Youth and Sports of the CR, CIISB - Czech Infrastructure for Integrative Structural Biology
MUNI/A/1313/2022, interní kód MUName: Podpora biochemického výzkumu v roce 2023
Investor: Masaryk University
MUNI/A/1604/2020, interní kód MUName: Podpora biochemického výzkumu v roce 2021
Investor: Masaryk University
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