{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zahler CT"],"funding":["American Chemical Society Petroleum Research Fund","Welch Foundation","National Science Foundation"],"pagination":["5364-5368"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6033162"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["57(19)"],"pubmed_abstract":["Determining whether a protein regulates its net electrostatic charge during electron transfer (ET) will deepen our mechanistic understanding of how polypeptides tune rates and free energies of ET (e.g., by affecting reorganization energy, and/or redox potential). Charge regulation during ET has never been measured for proteins because few tools exist to measure the net charge of a folded protein in solution at different oxidation states. Herein, we used a niche analytical tool (protein charge ladders analyzed with capillary electrophoresis) to determine that the net charges of myoglobin, cytochrome c, and azurin change by 0.62±0.06, 1.19±0.02, and 0.51±0.04 units upon single ET. Computational analysis predicts that these fluctuations in charge arise from changes in the pK<sub>a</sub>  valu"],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["Direct Measurement of Charge Regulation in Metalloprotein Electron Transfer."],"pmcid":["PMC6033162"],"funding_grant_id":["AA-1854","57521-DNI6","1352122"],"pubmed_authors":["Zahler CT","Shaw BF","Abdolvahabi A","Holden RL","Zhou H","Rasouli S","Tao P"],"additional_accession":[]},"is_claimable":false,"name":"Direct Measurement of Charge Regulation in Metalloprotein Electron Transfer.","description":"Determining whether a protein regulates its net electrostatic charge during electron transfer (ET) will deepen our mechanistic understanding of how polypeptides tune rates and free energies of ET (e.g., by affecting reorganization energy, and/or redox potential). Charge regulation during ET has never been measured for proteins because few tools exist to measure the net charge of a folded protein in solution at different oxidation states. Herein, we used a niche analytical tool (protein charge ladders analyzed with capillary electrophoresis) to determine that the net charges of myoglobin, cytochrome c, and azurin change by 0.62±0.06, 1.19±0.02, and 0.51±0.04 units upon single ET. Computational analysis predicts that these fluctuations in charge arise from changes in the pK<sub>a</sub>  valu","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 May","modification":"2026-05-05T23:15:16.383Z","creation":"2019-03-26T23:45:57Z"},"accession":"S-EPMC6033162","cross_references":{"pubmed":["29451960"],"doi":["10.1002/anie.201712306"]}}