دورية أكاديمية
أعرض في EDS

Structural Insight into Catalysis by the Flavin-Dependent NADH Oxidase (Pden_5119) of Paracoccus denitrificans .

التفاصيل البيبلوغرافية
العنوان: Structural Insight into Catalysis by the Flavin-Dependent NADH Oxidase (Pden_5119) of Paracoccus denitrificans .
المؤلفون: Kryl M; Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic., Sedláček V; Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic., Kučera I; Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, 61137 Brno, Czech Republic.
المصدر: International journal of molecular sciences [Int J Mol Sci] 2023 Feb 13; Vol. 24 (4). Date of Electronic Publication: 2023 Feb 13.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, [2000-
مواضيع طبية MeSH: Paracoccus denitrificans*/metabolism, NAD/metabolism ; Oxidation-Reduction ; Catalysis ; Flavins/chemistry ; Flavin Mononucleotide/chemistry ; Kinetics
مستخلص: 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 μM FMN while it contained only a descending limb pK a of 9.7 at 50 μM 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.
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معلومات مُعتمدة: GA 16-18476S Czech Science Foundation; MUNI/A/1604/2020 Grant Agency of Masaryk University; LM2018127 CIISB, Instruct-CZ Centre of Instruct-ERIC EU Consortium; CZ.02.1.01/0.0/0.0/18_046/0015974 European Regional Development Fund-Project "UP CIISB"
فهرسة مساهمة: Keywords: FMN; NADH; Paracoccus denitrificans; dioxygen reduction
المشرفين على المادة: EC 1.6.- (NADH oxidase)
0U46U6E8UK (NAD)
0 (Flavins)
7N464URE7E (Flavin Mononucleotide)
تواريخ الأحداث: Date Created: 20230225 Date Completed: 20230228 Latest Revision: 20230301
رمز التحديث: 20240829
مُعرف محوري في PubMed: PMC9963409
DOI: 10.3390/ijms24043732
PMID: 36835143
قاعدة البيانات: MEDLINE
الوصف
تدمد:1422-0067
DOI:10.3390/ijms24043732