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Article

Exploring the function of Tyr83 in bacteriorhodopsin: features of the Y83F and Y83N mutants.

Biochemistry - 6 Nov 2001

Imasheva E S, Lu M, Balashov S P, Ebrey T G, Chen Y, Ablonczy Z, Menick D R, Crouch R K

Abstract excerpt

Tyrosine-83, a residue which is conserved in all halobacterial retinal proteins, is located at the extracellular side in helix C of bacteriorhodopsin. Structural studies indicate that its hydroxyl group is hydrogen bonded to Trp189 and possibly to Glu194, a residue which is part of the proton release complex (PRC) in bacteriorhodopsin. To elucidate the role of Tyr83 in proton transport, we studied the Y83F and...

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Identifiers

PMID: 11683642
DOI: 10.1021/bi0110138

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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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