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Article

Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin.

Biochemistry - 22 Jul 1997

Balashov S P, Imasheva E S, Ebrey T G, Chen N, Menick D R, Crouch R K

Abstract excerpt

Substitution of glutamic acid-194, a residue on the extracellular surface of bacteriorhodopsin, with a cysteine inhibits the fast light-induced proton release that normally is coupled with the deprotonation of the Schiff base during the L to M transition. Proton release in this mutant occurs at the very end of the photocycle and coincides with deprotonation of the primary proton acceptor, Asp-85, during the O to...

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Identifiers

PMID: 9289012
DOI: 10.1021/bi970744y

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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.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin.PMID 9289012Read ↗

Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base.Semantic proximity Read ↗

Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base state.Semantic proximity Read ↗

Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.Semantic proximity Read ↗

Aspartate-histidine interaction in the retinal schiff base counterion of the light-driven proton pump of Exiguobacterium sibiricum.Semantic proximity Read ↗

Effects of mutations of Lys41 and Asp102 of bacteriorhodopsin.Semantic proximity Read ↗

Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it.Semantic proximity Read ↗

Photovoltage evidence that Glu-204 is the intermediate proton donor rather than the terminal proton release group in bacteriorhodopsin.Semantic proximity Read ↗

A redirected proton pathway in the bacteriorhodopsin mutant Tyr-57-->Asp. Evidence for proton translocation without Schiff base deprotonation.Semantic proximity Read ↗

Properties of Asp212----Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base.Semantic proximity Read ↗

L105K mutant of proteorhodopsin.Semantic proximity Read ↗

Photocycle in the M-form in bacteriorhodopsin mutants devoid of primary proton acceptor Asp-85.Semantic proximity Read ↗

Evidence for long range allosteric interactions between the extracellular and cytoplasmic parts of bacteriorhodopsin from the mutant R82A and its second site revertant R82A/G231C.Semantic proximity Read ↗

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