https://scholars.lib.ntu.edu.tw/handle/123456789/624876
標題: | Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO | 作者: | Lo F Hsieh C MANUEL MAESTRE-REYNA Chen C Ko T Horng Y Lai Y Chiang Y Chou C Chiang C Huang W Lin Y Bohle D.S Liaw W. |
關鍵字: | nitric oxide; non-heme diiron; protein structures; proteins | 公開日期: | 2016 | 卷: | 22 | 期: | 28 | 起(迄)頁: | 9768-9776 | 來源出版物: | Chemistry - A European Journal | 摘要: | Molecular mechanisms underlying the repair of nitrosylated [Fe–S] clusters by the microbial protein YtfE remain poorly understood. The X-ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and17O-labeling electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged FeII–FeIIIdiiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo-bridge. Structural analysis reveals that there are two solvent-accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates. The reactivity of the reduced-form FeII–FeIIYtfE toward nitric oxide demonstrates that the prerequisite for N2O production requires the two iron sites to be nitrosylated simultaneously. Specifically, the nitrosylation of the two iron sites prior to their reductive coupling to produce N2O is cooperative. This result suggests that, in addition to any repair of iron centers (RIC) activity, YtfE acts as an NO-trapping scavenger to promote the NO to N2O transformation under low NO flux, which precedes nitrosative stress. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84971384477&doi=10.1002%2fchem.201600990&partnerID=40&md5=5b1b0e6fd23cde8c4304fb06550d1367 https://scholars.lib.ntu.edu.tw/handle/123456789/624876 |
ISSN: | 09476539 | DOI: | 10.1002/chem.201600990 | SDG/關鍵字: | Amino acids; Carboxylation; Dichroism; Electron spin resonance spectroscopy; Magnetic moments; Nitric oxide; Proteins; Repair; Bridging carboxylates; Co-ordinatively unsaturated; Crystal structure analysis; Electron spin-echo envelope modulations; Magnetic circular dichroisms; non-heme diiron; Protein structures; X ray crystal structures; Crystal structure; iron; metalloprotein; nitric oxide; chemistry; circular dichroism; metabolism; molecular model; X ray crystallography; Circular Dichroism; Crystallography, X-Ray; Iron; Metalloproteins; Models, Molecular; Nitric Oxide |
顯示於: | 化學系 |
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