光解酶
化学
电子转移
色氨酸
结晶学
DNA
生物物理学
DNA修复
光化学
氨基酸
生物化学
生物
作者
Andrea Cellini,S. Madan Kumar,Amke Nimmrich,Leigh Anna Hunt,Leonardo Monrroy,Jennifer Mutisya,Antonia Furrer,Emma V. Beale,Melissa Carrillo,Tek Narsingh Malla,Piotr Maj,Lidija Vrhovac,Florian Dworkowski,Claudio Cirelli,Philip J. M. Johnson,D. Ozerov,Emina A. Stojković,Leif Hammarström,Camila Bacellar,Jörg Standfuss
出处
期刊:Nature Chemistry
[Nature Portfolio]
日期:2024-01-15
卷期号:16 (4): 624-632
被引量:21
标识
DOI:10.1038/s41557-023-01413-9
摘要
Abstract Charge-transfer reactions in proteins are important for life, such as in photolyases which repair DNA, but the role of structural dynamics remains unclear. Here, using femtosecond X-ray crystallography, we report the structural changes that take place while electrons transfer along a chain of four conserved tryptophans in the Drosophila melanogaster (6-4) photolyase. At femto- and picosecond delays, photoreduction of the flavin by the first tryptophan causes directed structural responses at a key asparagine, at a conserved salt bridge, and by rearrangements of nearby water molecules. We detect charge-induced structural changes close to the second tryptophan from 1 ps to 20 ps, identifying a nearby methionine as an active participant in the redox chain, and from 20 ps around the fourth tryptophan. The photolyase undergoes highly directed and carefully timed adaptations of its structure. This questions the validity of the linear solvent response approximation in Marcus theory and indicates that evolution has optimized fast protein fluctuations for optimal charge transfer.
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