Influence of QA site redox cofactor structure on equilibrium binding, in situ electrochemistry, and electron-transfer performance in the photosynthetic reaction center protein
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00069a011
Reference68 articles.
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3. One- and two-electron reduction of hydroxy-1,4-naphthoquinones and hydroxy-9,10-anthraquinones
4. Dynamics of ligand binding to myoglobin
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2. Modulating the lifetime of the charge-separated state in photosynthetic reaction center by out-of-protein electrostatics;MRS Advances;2018-03-01
3. Affinity and activity of non-native quinones at the QB site of bacterial photosynthetic reaction centers;Photosynthesis Research;2013-05-29
4. Slow Dissociation of a Charged Ligand: Analysis of the Primary Quinone QA Site of Photosynthetic Bacterial Reaction Centers;Journal of the American Chemical Society;2011-10-11
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