Structural basis of the radical pair state in photolyases and cryptochromes

Cellini, Andrea; Shankar, Madan Kumar; Wahlgren, Weixiao Yuan; Nimmrich, Amke; Furrer, Antonia; James, Daniel; Wranik, Maximilian; Aumonier, Sylvain; Beale, Emma V.; Dworkowski, Florian; Standfuss, Jörg; Weinert, T.; Westenhoff, Sebastian

doi:10.1039/d2cc00376g

Cited by 10 publications

(24 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The DED around Trp381 is weaker than what we detected previously at 100 ms, but features appear at similar positions (Fig. S5) [35].…”

Section: Resultssupporting

confidence: 59%

“…We now turn our attention to changes along the tryptophan tetrad. As in the previous serial crystallographic experiments on photolyases [34,35],…”

Section: Resultsmentioning

confidence: 73%

“…4B). At 100 µs, we detect structural changes at Trp381, Pro329, Asn490 and Met494, indicating that the hydrogen bond between Pro329 and Trp381 in the dark state breaks [35], that the side chain of Trp381 moves, and that Asn490 is moving closer to Trp381. We interpret these changes to be due to the arrival of the charge to the last tryptophan Trp381.…”

Section: Resultsmentioning

confidence: 95%

“…The technique has been used for deciphering structural mechanisms in photosynthetic, sensor, and transport proteins [28][29][30][31][32][33]. With respect to photolyases, a nanosecond time-resolved SFX study has been carried for the two reduction steps on a cis-syn cyclobutane pyrimidine dimer (CBD) photolyase [34], and we have recorded a crystallographic snapshot of the end state of the first photoreduction in a (6-4) photolyase at 100 ms [35]. Here, we capture structural snapshots for the (6-4) photolyase from Drosophila Melanogaster covering the earliest, femto-and picosecond time scales.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Femtosecond conformational changes in a photolyase guide long-range electron transfer as resolved by serial crystallography

Cellini

Shankar

Nimmrich

et al. 2023

Preprint

View full text Add to dashboard Cite

Charge transfer reactions in proteins are fundamentally important for life, but it is currently not clear how protein structural dynamics control these electron transfer reactions. Photolyases/cryptochromes, which repair DNA and signal in all kingdoms of life, have a paradigm electron transfer cascade. Here, photoreduction of the flavin cofactor initiates charge transfer along a chain of four conserved tryptophans. We report femtosecond X-ray crystallographic snap-shots for the Drosophila melanogaster (6-4) photolyase, revealing protein structural changes while electron transfer occurs. At femto- and picosecond delays, photoreduction of the flavin by the first tryptophan causes directed structural responses at key residue asparagine 403, at a conserved salt bridge, and by rearrangements of nearby water molecules. Along the tryptophan cascade, we detect charge-induced protein structural changes close to the second tryptophan from 1 ps to 20 ps, thereby identifying methionine 408 as an active participant in the redox chain, and from 300 ps around the fourth tryptophan. The data reveal that the protein undergoes highly directed and carefully timed adaptations of its structure to facilitate electron transfer. This suggests that evolution has optimized fast protein fluctuations for optimal function.

show abstract

“…The DED around Trp381 is weaker than what we detected previously at 100 ms, but features appear at similar positions (Fig. S5) [35].…”

Section: Resultssupporting

confidence: 59%

“…We now turn our attention to changes along the tryptophan tetrad. As in the previous serial crystallographic experiments on photolyases [34,35],…”

Section: Resultsmentioning

confidence: 73%

Section: Resultsmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Femtosecond conformational changes in a photolyase guide long-range electron transfer as resolved by serial crystallography

Cellini

Shankar

Nimmrich

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

“…The flavin radical can also be formed as a result of the oxidation of the photoexcited flavin dihydroform; this reaction is the basis for the functioning of DNA photolyases (see below) [ 221 , 222 ]. Additional stability of the flavin radical can be imparted by amino acids that surround the flavin in the reaction center of the protein [ 223 , 224 ].…”

Section: Biochemical and Physiological Application Of Pterin Photoche...mentioning

confidence: 99%

Insights into Molecular Structure of Pterins Suitable for Biomedical Applications

Buglak

Kapitonova

Vechtomova

et al. 2022

IJMS

View full text Add to dashboard Cite

Pterins are an inseparable part of living organisms. Pterins participate in metabolic reactions mostly as tetrahydropterins. Dihydropterins are usually intermediates of these reactions, whereas oxidized pterins can be biomarkers of diseases. In this review, we analyze the available data on the quantum chemistry of unconjugated pterins as well as their photonics. This gives a comprehensive overview about the electronic structure of pterins and offers some benefits for biomedicine applications: (1) one can affect the enzymatic reactions of aromatic amino acid hydroxylases, NO synthases, and alkylglycerol monooxygenase through UV irradiation of H4pterins since UV provokes electron donor reactions of H4pterins; (2) the emission properties of H2pterins and oxidized pterins can be used in fluorescence diagnostics; (3) two-photon absorption (TPA) should be used in such pterin-related infrared therapy because single-photon absorption in the UV range is inefficient and scatters in vivo; (4) one can affect pathogen organisms through TPA excitation of H4pterin cofactors, such as the molybdenum cofactor, leading to its detachment from proteins and subsequent oxidation; (5) metal nanostructures can be used for the UV-vis, fluorescence, and Raman spectroscopy detection of pterin biomarkers. Therefore, we investigated both the biochemistry and physical chemistry of pterins and suggested some potential prospects for pterin-related biomedicine.

show abstract

Quantum Biology of Circadian Rhythms

Moazed

2023

Quantum Biology of the Eye

View full text Add to dashboard Cite

Structural basis of the radical pair state in photolyases and cryptochromes

Abstract: We present the structure of a photoactivated animal (6-4) photolyase in its radical pair state, captured by serial crystallography. We observe how a conserved asparigine moves towards the semiquinone FAD...

Cited by 10 publications

References 42 publications

Femtosecond conformational changes in a photolyase guide long-range electron transfer as resolved by serial crystallography

Femtosecond conformational changes in a photolyase guide long-range electron transfer as resolved by serial crystallography

Insights into Molecular Structure of Pterins Suitable for Biomedical Applications

Quantum Biology of Circadian Rhythms

Contact Info

Product

Resources

About