{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sugo Y"],"funding":["University of Tsukuba","Japan Society for the Promotion of Science"],"pagination":["1544-1552"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10194076"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["62(10)"],"pubmed_abstract":["In photosynthetic reaction centers from purple bacteria (PbRCs), light-induced charge separation leads to the reduction of the terminal electron acceptor quinone, Q<sub>B</sub>. The reduction of Q<sub>B</sub> to Q<sub>B</sub><sup>•-</sup> is followed by protonation via Asp-L213 and Ser-L223 in PbRC from <i>Rhodobacter sphaeroides</i>. However, Asp-L213 is replaced with nontitratable Asn-L222 and Asn-L213 in PbRCs from <i>Thermochromatium tepidum</i> and <i>Blastochloris viridis</i>, respectively. Here, we investigated the energetics of proton transfer along the asparagine-involved H-bond network using a quantum mechanical/molecular mechanical approach. The potential energy profile for the H-bond between H<sub>3</sub>O<sup>+</sup> and the carbonyl O site of Asn-L222 shows that the proton is"],"journal":["Biochemistry"],"pubmed_title":["Mechanism of Asparagine-Mediated Proton Transfer in Photosynthetic Reaction Centers."],"pmcid":["PMC10194076"],"funding_grant_id":["JP20H05090","JP20H03217","JP18H01937","JP18H05155"],"pubmed_authors":["Sugo Y","Ishikita H"],"additional_accession":[]},"is_claimable":false,"name":"Mechanism of Asparagine-Mediated Proton Transfer in Photosynthetic Reaction Centers.","description":"In photosynthetic reaction centers from purple bacteria (PbRCs), light-induced charge separation leads to the reduction of the terminal electron acceptor quinone, Q<sub>B</sub>. The reduction of Q<sub>B</sub> to Q<sub>B</sub><sup>•-</sup> is followed by protonation via Asp-L213 and Ser-L223 in PbRC from <i>Rhodobacter sphaeroides</i>. However, Asp-L213 is replaced with nontitratable Asn-L222 and Asn-L213 in PbRCs from <i>Thermochromatium tepidum</i> and <i>Blastochloris viridis</i>, respectively. Here, we investigated the energetics of proton transfer along the asparagine-involved H-bond network using a quantum mechanical/molecular mechanical approach. The potential energy profile for the H-bond between H<sub>3</sub>O<sup>+</sup> and the carbonyl O site of Asn-L222 shows that the proton is","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2026-05-28T21:54:31.89Z","creation":"2026-04-08T03:17:15.427Z"},"accession":"S-EPMC10194076","cross_references":{"pubmed":["37083399"],"doi":["10.1021/acs.biochem.3c00013"]}}