Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography.

Autor: Cellini A; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden., Shankar MK; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.; Department of Chemistry - BMC, Uppsala University, Uppsala, Sweden., Nimmrich A; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.; Department of Chemistry, University of Washington, Seattle, WA, USA., Hunt LA; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden., Monrroy L; Department of Chemistry - BMC, Uppsala University, Uppsala, Sweden., Mutisya J; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.; Department of Chemistry - BMC, Uppsala University, Uppsala, Sweden., Furrer A; Paul Scherrer Institut, Villigen, Switzerland., Beale EV; Paul Scherrer Institut, Villigen, Switzerland., Carrillo M; Paul Scherrer Institut, Villigen, Switzerland., Malla TN; Physics Department, University of Wisconsin-Milwaukee, Milwaukee, WI, USA., Maj P; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.; Department of Chemistry - BMC, Uppsala University, Uppsala, Sweden., Vrhovac L; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.; Department of Chemistry - BMC, Uppsala University, Uppsala, Sweden., Dworkowski F; Paul Scherrer Institut, Villigen, Switzerland., Cirelli C; Paul Scherrer Institut, Villigen, Switzerland., Johnson PJM; Paul Scherrer Institut, Villigen, Switzerland., Ozerov D; Paul Scherrer Institut, Villigen, Switzerland., Stojković EA; Department of Biology, Northeastern Illinois University, Chicago, IL, USA., Hammarström L; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden., Bacellar C; Paul Scherrer Institut, Villigen, Switzerland., Standfuss J; Paul Scherrer Institut, Villigen, Switzerland., Maj M; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden., Schmidt M; Physics Department, University of Wisconsin-Milwaukee, Milwaukee, WI, USA., Weinert T; Paul Scherrer Institut, Villigen, Switzerland., Ihalainen JA; Department of Biological and Environmental Sciences, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland., Wahlgren WY; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.; Department of Chemistry and Molecular Biology and the Swedish NMR Centre, University of Gothenburg, Gothenburg, Sweden., Westenhoff S; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden. sebastian.westenhoff@kemi.uu.se.; Department of Chemistry - BMC, Uppsala University, Uppsala, Sweden. sebastian.westenhoff@kemi.uu.se.
Jazyk: angličtina
Zdroj: Nature chemistry [Nat Chem] 2024 Apr; Vol. 16 (4), pp. 624-632. Date of Electronic Publication: 2024 Jan 15.
DOI: 10.1038/s41557-023-01413-9
Abstrakt: 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.
(© 2024. The Author(s).)
Databáze: MEDLINE
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