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Article

Proton transfer dynamics on the surface of the late M state of bacteriorhodopsin.

Biophysical journal - 1 Jul 2002

Nachliel Esther, Gutman Menachem, Tittor Jörg, Oesterhelt Dieter

Abstract excerpt

The cytoplasmic surface of the BR (initial) state of bacteriorhodopsin is characterized by a cluster of three carboxylates that function as a proton-collecting antenna. Systematic replacement of most of the surface carboxylates indicated that the cluster is made of D104, E161, and E234 (Checover, S., Y. Marantz, E. Nachliel, M. Gutman, M. Pfeiffer, J. Tittor, D. Oesterhelt, and N. Dencher. 2001. Biochemistry....

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Identifiers

PMID: 12080130
DOI: 10.1016/S0006-3495(02)75179-5
PMCID: PMC1302157

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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