دورية أكاديمية
Active Site Characterization of a Campylobacter jejuni Nitrate Reductase Variant Provides Insight into the Enzyme Mechanism.
العنوان: | Active Site Characterization of a Campylobacter jejuni Nitrate Reductase Variant Provides Insight into the Enzyme Mechanism. |
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المؤلفون: | Yang J; Department of Chemistry and Chemical Biology, The University of New Mexico, MSC03 2060, 1 University of New Mexico, Albuquerque, New Mexico 87131-0001, United States., Mintmier B; Department of Chemistry and Chemical Biology, Indiana University, 402 Blackford St., Indianapolis, Indiana 46202, United States., Kc K; Department of Chemistry and Chemical Biology, The University of New Mexico, MSC03 2060, 1 University of New Mexico, Albuquerque, New Mexico 87131-0001, United States., Metzger MC; Department of Chemistry and Chemical Biology, Indiana University, 402 Blackford St., Indianapolis, Indiana 46202, United States., Radhakrishnan M; Department of Chemistry and Chemical Biology, Indiana University, 402 Blackford St., Indianapolis, Indiana 46202, United States., McGarry J; Department of Chemistry and Chemical Biology, Indiana University, 402 Blackford St., Indianapolis, Indiana 46202, United States.; Department of Chemistry and Biochemistry, University of Wisconsin, 3210 N. Cramer St., Milwaukee, Wisconsin 53211, United States., Wilcoxen J; Department of Chemistry and Biochemistry, University of Wisconsin, 3210 N. Cramer St., Milwaukee, Wisconsin 53211, United States., Basu P; Department of Chemistry and Chemical Biology, Indiana University, 402 Blackford St., Indianapolis, Indiana 46202, United States., Kirk ML; Department of Chemistry and Chemical Biology, The University of New Mexico, MSC03 2060, 1 University of New Mexico, Albuquerque, New Mexico 87131-0001, United States. |
المصدر: | Inorganic chemistry [Inorg Chem] 2024 Jul 22; Vol. 63 (29), pp. 13191-13196. Date of Electronic Publication: 2024 Jul 10. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0366543 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-510X (Electronic) Linking ISSN: 00201669 NLM ISO Abbreviation: Inorg Chem Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: [Easton, Pa.] American Chemical Society. |
مواضيع طبية MeSH: | Campylobacter jejuni*/enzymology , Nitrate Reductase*/chemistry , Nitrate Reductase*/metabolism , Catalytic Domain*, Models, Molecular ; X-Ray Absorption Spectroscopy |
مستخلص: | Mo K-edge X-ray absorption spectroscopy (XAS) is used to probe the structure of wild-type Campylobacter jejuni nitrate reductase NapA and the C176A variant. The results of extended X-ray absorption fine structure (EXAFS) experiments on wt NapA support an oxidized Mo(VI) hexacoordinate active site coordinated by a single terminal oxo donor, four sulfur atoms from two separate pyranopterin dithiolene ligands, and an additional S atom from a conserved cysteine amino acid residue. We found no evidence of a terminal sulfido ligand in wt NapA. EXAFS analysis shows the C176A active site to be a 6-coordinate structure, and this is supported by EPR studies on C176A and small molecule analogs of Mo(V) enzyme forms. The S |
المشرفين على المادة: | EC 1.7.99.4 (Nitrate Reductase) |
تواريخ الأحداث: | Date Created: 20240710 Date Completed: 20240722 Latest Revision: 20240722 |
رمز التحديث: | 20240722 |
DOI: | 10.1021/acs.inorgchem.4c01991 |
PMID: | 38984973 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1520-510X |
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DOI: | 10.1021/acs.inorgchem.4c01991 |