@article {27326,
	title = {Serial crystallography captures dynamic control of sequential electron and proton transfer events in a flavoenzyme},
	journal = {Nature Chemistry},
	volume = {14},
	number = {6},
	year = {2022},
	note = {Export Date: 06 April 2024; Cited By: 21},
	month = {2022},
	pages = {677 - 685},
	abstract = {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{\textbullet}- isoalloxazine ring twists strongly when the arginine closes in to stabilize the negative charge. Subsequent breakage of the arginine{\textendash}aspartate salt bridge allows proton transfer from arginine to FAD{\textbullet}-. 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.] {\textcopyright} 2022, The Author(s), under exclusive licence to Springer Nature Limited.},
	url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85127648859\&doi=10.1038\%2fs41557-022-00922-3\&partnerID=40\&md5=65afb613e670bbbcb95aa5e0e2d5c5a5},
	author = {Maestre-Reyna, M. and Yang, C.-H. and Nango, E. and Huang, W.-C. and Ngurah Putu, E.P.G. and Wu, W.-J. and Wang, P.-H. and Franz-Badur, S. and Saft, M. and Emmerich, H.-J. and Wu, H.-Y. and Lee, C.-C. and Huang, K.-F. and Chang, Y.-K. and Liao, J.-H. and Weng, J.-H. and Gad, W. and Chang, C.-W. and Pang, A.H. and Sugahara, M. and Owada, S. and Hosokawa, Y. and Joti, Y. and Yamashita, A. and Tanaka, R. and Tanaka, T. and Luo, F. and Tono, K. and Hsu, K.-C. and Kiontke, S. and Schapiro, I. and Spadaccini, R. and Royant, A. and Yamamoto, J. and Iwata, S. and Essen, L.-O. and Bessho, Y. and Tsai, M.-D.}
}
