{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhou Y"],"funding":["Ministry of Science and Technology of the People’s Republic of China","National Natural Science Foundation of China","Ministry of Science and Technology of the People's Republic of China (Chinese Ministry of Science and Technology)","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["623"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10799861"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Blue light using flavin (BLUF) photoreceptors respond to light via one of nature's smallest photo-switching domains. Upon photo-activation, the flavin cofactor in the BLUF domain exhibits multi-phasic dynamics, quenched by a proton-coupled electron transfer reaction involving the conserved Tyr and Gln. The dynamic behavior varies drastically across different species, the origin of which remains controversial. Here, we incorporate site-specific fluorinated Trp into three BLUF proteins, i.e., AppA, OaPAC and SyPixD, and characterize the percentages for the W<sub>out</sub>, W<sub>in</sub>NH<sub>in</sub> and W<sub>in</sub>NH<sub>out</sub> conformations using <sup>19</sup>F nuclear magnetic resonance spectroscopy. Using femtosecond spectroscopy, we identify that one key W<sub>in</sub>NH<sub>in<"],"journal":["Nature communications"],"pubmed_title":["Origin of the multi-phasic quenching dynamics in the BLUF domains across the species."],"pmcid":["PMC10799861"],"funding_grant_id":["31971233","2020YFA0509700"],"pubmed_authors":["Zhang T","Ding B","Chen Z","Huang J","Wang B","Kang XW","Zhong D","Tang S","Zou S","Zhou Y","Zhou Z"],"additional_accession":[]},"is_claimable":false,"name":"Origin of the multi-phasic quenching dynamics in the BLUF domains across the species.","description":"Blue light using flavin (BLUF) photoreceptors respond to light via one of nature's smallest photo-switching domains. Upon photo-activation, the flavin cofactor in the BLUF domain exhibits multi-phasic dynamics, quenched by a proton-coupled electron transfer reaction involving the conserved Tyr and Gln. The dynamic behavior varies drastically across different species, the origin of which remains controversial. Here, we incorporate site-specific fluorinated Trp into three BLUF proteins, i.e., AppA, OaPAC and SyPixD, and characterize the percentages for the W<sub>out</sub>, W<sub>in</sub>NH<sub>in</sub> and W<sub>in</sub>NH<sub>out</sub> conformations using <sup>19</sup>F nuclear magnetic resonance spectroscopy. Using femtosecond spectroscopy, we identify that one key W<sub>in</sub>NH<sub>in<","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jan","modification":"2026-06-03T01:41:58.818Z","creation":"2024-10-15T23:59:45.15Z"},"accession":"S-EPMC10799861","cross_references":{"pubmed":["38245518"],"doi":["10.1038/s41467-023-44565-5"]}}