The Proton Release Group of Bacteriorhodopsin Controls the Rate of the Final Step of Its Photocycle at Low pH

Author:

Balashov Sergei P.1,Lu Miao1,Imasheva Eleonora S.1,Govindjee Rajni1,Ebrey Thomas G.1,Othersen Beimann1,Chen Yumei1,Crouch Rosalie K.1,Menick Donald R.1

Affiliation:

1. Center for Biophysics and Computational Biology and Department of Cell and Structural Biology, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801, and Medical University of South Carolina, Charleston, South Carolina 29425

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

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1. Optimization of nonequilibrium free energy harvesting illustrated on bacteriorhodopsin;Physical Review Research;2024-03-12

2. Existence of two substates in the O intermediate of the bacteriorhodopsin photocycle;Biochimica et Biophysica Acta (BBA) - Biomembranes;2022-10

3. Proton transfer reactions in donor site mutants of ESR, a retinal protein from Exiguobacterium sibiricum;Journal of Photochemistry and Photobiology B: Biology;2022-09

4. Amino acid deprotonation rates from classical force fields;The Journal of Chemical Physics;2022-08-28

5. O to bR transition in bacteriorhodopsin occurs through a proton hole mechanism;Proceedings of the National Academy of Sciences;2021-09-24

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