Multielectron Chemistry within a Model Nickel Metalloprotein: Mechanistic Implications for Acetyl-CoA Synthase.

التفاصيل البيبلوغرافية
العنوان:	Multielectron Chemistry within a Model Nickel Metalloprotein: Mechanistic Implications for Acetyl-CoA Synthase.
المؤلفون:	Manesis AC; The Ohio State University , 100 West 18th Avenue, Newman & Wolfrom Laboratory of Chemistry, Columbus, Ohio 43210, United States., O'Connor MJ; The Ohio State University , 100 West 18th Avenue, Newman & Wolfrom Laboratory of Chemistry, Columbus, Ohio 43210, United States., Schneider CR; The Ohio State University , 100 West 18th Avenue, Newman & Wolfrom Laboratory of Chemistry, Columbus, Ohio 43210, United States., Shafaat HS; The Ohio State University , 100 West 18th Avenue, Newman & Wolfrom Laboratory of Chemistry, Columbus, Ohio 43210, United States.
المصدر:	Journal of the American Chemical Society [J Am Chem Soc] 2017 Aug 02; Vol. 139 (30), pp. 10328-10338. Date of Electronic Publication: 2017 Jul 21.
نوع المنشور:	Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة:	English
بيانات الدورية:	Publisher: American Chemical Society Country of Publication: United States NLM ID: 7503056 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5126 (Electronic) Linking ISSN: 00027863 NLM ISO Abbreviation: J Am Chem Soc Subsets: MEDLINE
أسماء مطبوعة:	Publication: Washington, DC : American Chemical Society Original Publication: Easton, Pa. [etc.]
مواضيع طبية MeSH:	Acetate-CoA Ligase/metabolism , Carbon Monoxide/chemistry , Metalloproteins/chemistry , Nickel/chemistry, Acetate-CoA Ligase/chemistry ; Carbon Monoxide/metabolism ; Electrons ; Metalloproteins/isolation & purification ; Metalloproteins/metabolism ; Models, Molecular ; Nickel/metabolism ; Oxidation-Reduction ; Pseudomonas aeruginosa/enzymology
مستخلص:	The acetyl coenzyme A synthase (ACS) enzyme plays a central role in the metabolism of anaerobic bacteria and archaea, catalyzing the reversible synthesis of acetyl-CoA from CO and a methyl group through a series of nickel-based organometallic intermediates. Owing to the extreme complexity of the native enzyme systems, the mechanism by which this catalysis occurs remains poorly understood. In this work, we have developed a protein-based model for the Ni P center of acetyl coenzyme A synthase using a nickel-substituted azurin protein (NiAz). NiAz is the first model nickel protein system capable of accessing three (Ni ^I /Ni ^II /Ni ^III ) distinct oxidation states within a physiological potential range in aqueous solution, a critical feature for achieving organometallic ACS activity, and binds CO and -CH 3 groups with biologically relevant affinity. Characterization of the Ni ^I -CO species through spectroscopic and computational techniques reveals fundamentally similar features between the model NiAz system and the native ACS enzyme, highlighting the potential for related reactivity in this model protein. This work provides insight into the enzymatic process, with implications toward engineering biological catalysts for organometallic processes.
المشرفين على المادة:	0 (Metalloproteins) 7OV03QG267 (Nickel) 7U1EE4V452 (Carbon Monoxide) EC 6.2.1.1 (Acetate-CoA Ligase)
تواريخ الأحداث:	Date Created: 20170706 Date Completed: 20180531 Latest Revision: 20180531
رمز التحديث:	20240628
DOI:	10.1021/jacs.7b03892
PMID:	28675928
قاعدة البيانات:	MEDLINE

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الوصف
تدمد:	1520-5126
DOI:	10.1021/jacs.7b03892