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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chou, Chih-mao Horng, Yih-chern Lai, Yei-chen Chen, Chin-yu Chiang, Cheng-hung Hsieh, Chang-chih Bohle, D. Scott Liaw, Wen-feng Chiang, Yun-wei Lo, Feng-chun Huang, Wei-ning Maestre-reyna, Manuel Ko, Tzu-ping Lin, Yi-hung |
| Description | Author Affiliation: Lo FC ( Department of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan.); Hsieh CC ( Department of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan.); Maestre-Reyna M ( Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan. mmaestre@gate.sinica.edu.tw.); Chen CY ( Department of Life Sciences, National Central University, Taoyuan, Taiwan. chinyuchen@cc.ncu.edu.tw.); Ko TP ( Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.); Horng YC ( Department of Chemistry, National Changhua University of Education, Changhua, Taiwan.); Lai YC ( Department of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan.); Chiang YW ( Department of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan. ywchiang@mx.nthu.edu.tw.); Chou CM ( Department of Life Sciences, National Central University, Taoyuan, Taiwan.); Chiang CH ( National Synchrotron Radiation Research Center Hsinchu, Taiwan.); Huang WN ( Department of Biotechnology, Yuanpei University, Hsinchu, Taiwan.); Lin YH ( National Synchrotron Radiation Research Center Hsinchu, Taiwan.); Bohle DS ( Department of Chemistry, McGill University, 801 Sherbrooke Street West, Montreal, QC, H3A2K6, Canada. scott.bohle@mcgill.ca.); Liaw WF ( Department of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan. wfliaw@mx.nthu.edu.tw.) |
| Abstract | 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, and $^{17}O-labeling$ electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged $Fe^{II}–Fe^{III}$ diiron 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 $Fe^{II}–Fe^{II}$ YtfE toward nitric oxide demonstrates that the prerequisite for $N_{2}O$ 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 $N_{2}O$ 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 $N_{2}O$ transformation under low NO flux, which precedes nitrosative stress. |
| ISSN | 09476539 |
| e-ISSN | 15213765 |
| Journal | Chemistry - A European Journal |
| Issue Number | 28 |
| Volume Number | 22 |
| Language | English |
| Publisher | Wiley-VCH;ChemPubSoc Europe |
| Publisher Date | 2016-07-04 |
| Publisher Place | Germany |
| Access Restriction | Open |
| Subject Keyword | Chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Catalysis |
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