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Article

Critical role of Asp227 in the photocycle of proteorhodopsin.

Biochemistry - 17 Jul 2012

Herz Julia, Verhoefen Mirka-Kristin, Weber Ingrid, Bamann Christian, Glaubitz Clemens, Wachtveitl Josef

Abstract excerpt

The photocycle of the proton acceptor complex mutant D227N of the bacterial retinal protein proteorhodopsin is investigated employing steady state pH-titration experiments in the UV-visible range as well as femtosecond-pump-probe spectroscopy and flash photolysis in the visible spectral range. The evaluation of the pH-dependent spectra showed that the neutralization of the charge at position 227 has a remarkable...

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PMID: 22738119
DOI: 10.1021/bi3003764

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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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Critical role of Asp227 in the photocycle of proteorhodopsin.PMID 22738119Read ↗

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 ↗

In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy.Semantic proximity Read ↗

Proton transport by proteorhodopsin requires that the retinal Schiff base counterion Asp-97 be anionic.Semantic proximity Read ↗

The EF loop in green proteorhodopsin affects conformation and photocycle dynamics.Semantic proximity Read ↗

Primary reaction dynamics of proteorhodopsin mutant D97N observed by femtosecond infrared and visible spectroscopy.Semantic proximity Read ↗

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

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