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Article

Crystal structures of bR(D85S) favor a model of bacteriorhodopsin as a hydroxyl-ion pump.

FEBS letters - 30 Apr 2004

Facciotti Marc T, Rouhani Shahab, Glaeser Robert M

Abstract excerpt

Structural features on the extracellular side of the D85S mutant of bacteriorhodopsin (bR) suggest that wild-type bR could be a hydroxyl-ion pump. A position between the protonated Schiff base and residue 85 serves as an anion-binding site in the mutant protein, and hydroxyl ions should have access to this site during the O-intermediate of the wild-type bR photocycle. The guanidinium group of R82 is proposed (1)...

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Identifiers

PMID: 15111113
DOI: 10.1016/S0014-5793(04)00208-X

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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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