Deprotonation of the Schiff Base of Rhodopsin Is Obligate in the Activation of the G Protein.

Proceedings of the National Academy of Sciences of the United States of America- United States

doi 10.1073/pnas.83.12.4209

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Abstract

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Date

June 1, 1986

Authors

C. Longstaff

R. D. Calhoon

R. R. Rando

Publisher

Proceedings of the National Academy of Sciences

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Deprotonation of the Schiff Base of Rhodopsin Is Obligate in the Activation of the G Protein.

Proceedings of the National Academy of Sciences of the United States of America- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

On the Molecular Mechanisms of the Schiff Base Deprotonation During the Bacteriorhodopsin Photocycle

pKa of the Protonated Schiff Base of Bovine Rhodopsin. A Study With Artificial Pigments

Evidence for the Involvement of More Than One Metal Cation in the Schiff Base Deprotonation Process During the Photocycle of Bacteriorhodopsin

What Site-Directed Labeling Studies Tell Us About the Mechanism of Rhodopsin Activation and G-Protein Binding

3P240 the Proton Donor for the Schiff Base Is Perturbed Upon Retinal Photoisomerization in Gloeobacter Rhodopsin(Photobiology- Vision and Photoreception. Actinobiology,Oral Presentations)

Two-Photon Spectroscopy of Locked-11-Cis-Rhodopsin: Evidence for a Protonated Schiff Base in a Neutral Protein Binding Site.

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Aspartic Acid-96 Is the Internal Proton Donor in the Reprotonation of the Schiff Base of Bacteriorhodopsin.

Energetic Analysis of the Rhodopsin–G-Protein Complex Links the Α5 Helix to GDP Release