https://scholars.lib.ntu.edu.tw/handle/123456789/624866
標題: | Serial crystallography captures dynamic control of sequential electron and proton transfer events in a flavoenzyme | 作者: | MANUEL MAESTRE-REYNA Yang C.-H Nango E Huang W.-C Ngurah Putu E.P.G Wu W.-J Wang P.-H Franz-Badur S Saft M Emmerich H.-J Wu H.-Y Lee C.-C Huang K.-F Chang Y.-K Liao J.-H Weng J.-H Gad W Chang C.-W Pang A.H Sugahara M Owada S Hosokawa Y Joti Y Yamashita A Tanaka R Tanaka T Luo F Tono K Hsu K.-C Kiontke S Schapiro I Spadaccini R Royant A Yamamoto J Iwata S Essen L.-O Bessho Y Tsai M.-D. |
公開日期: | 2022 | 卷: | 14 | 期: | 6 | 起(迄)頁: | 677-685 | 來源出版物: | Nature Chemistry | 摘要: | Flavin coenzymes are universally found in biological redox reactions. DNA photolyases, with their flavin chromophore (FAD), utilize blue light for DNA repair and photoreduction. The latter process involves two single-electron transfers to FAD with an intermittent protonation step to prime the enzyme active for DNA repair. Here we use time-resolved serial femtosecond X-ray crystallography to describe how light-driven electron transfers trigger subsequent nanosecond-to-microsecond entanglement between FAD and its Asn/Arg-Asp redox sensor triad. We found that this key feature within the photolyase-cryptochrome family regulates FAD re-hybridization and protonation. After first electron transfer, the FAD•− isoalloxazine ring twists strongly when the arginine closes in to stabilize the negative charge. Subsequent breakage of the arginine–aspartate salt bridge allows proton transfer from arginine to FAD•−. Our molecular videos demonstrate how the protein environment of redox cofactors organizes multiple electron/proton transfer events in an ordered fashion, which could be applicable to other redox systems such as photosynthesis. [Figure not available: see fulltext.] © 2022, The Author(s), under exclusive licence to Springer Nature Limited. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85127648859&doi=10.1038%2fs41557-022-00922-3&partnerID=40&md5=65afb613e670bbbcb95aa5e0e2d5c5a5 https://scholars.lib.ntu.edu.tw/handle/123456789/624866 |
ISSN: | 17554330 | DOI: | 10.1038/s41557-022-00922-3 | SDG/關鍵字: | arginine; deoxyribodipyrimidine photolyase; flavine adenine nucleotide; proton; quercetin; chemistry; crystallography; electron; electron transport; genetics; metabolism; oxidation reduction reaction; Arginine; Crystallography; Deoxyribodipyrimidine Photo-Lyase; Electron Transport; Electrons; Flavin-Adenine Dinucleotide; Flavins; Oxidation-Reduction; Protons |
顯示於: | 化學系 |
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