13-Acetoxy-13-desmethylretinal: Synthesis incorporation into bacteriorhodopsin, and its apparent inactivating effect

Journal Article · Wed Oct 05 04:00:00 EDT 1994 · Journal of the American Chemical Society; (United States)

DOI:https://doi.org/10.1021/ja00099a087· OSTI ID:6768256

Seltzer, S ^[1]

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1. Brookhaven National Lab., Upton, NY (United States)

Bacteriorhodopsin (bR), the protein pigment of the purple membrane (PM) light-driven proton pump, is a single polypeptide chain of 248 amino acids. It traverses the membrane to form seven rods of high [alpha]-helical character. PM's color results from the presence of an equivalent of retinal, bound as a protonated Schiff base (PRSB) at lysine 216, and its interaction with the protein. Light initiates a photocycle where the first step is a photoisomerization of all-trans-retinal to the 13-cis isomer. All subsequent steps in the cycle are thermal dark reactions. We report herein the synthesis and incorporation into bacteriorhodopsin of a novel analogue, 13-acetoxy-13-desmethylretinal designed to probe the mechanism of dark cis-trans isomerization. 24 refs., 1 fig.

• DOE Contract Number: AC02-76CH00016
• OSTI ID: 6768256
• Journal Information: Journal of the American Chemical Society; (United States), Journal Name: Journal of the American Chemical Society; (United States) Vol. 116:20; ISSN JACSAT; ISSN 0002-7863
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400201* -- Chemical & Physicochemical Properties
400500 -- Photochemistry
550200 -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALDEHYDES
AMINO ACIDS
BACTERIA
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
DERIVATIZATION
IONIZATION
MEMBRANE PROTEINS
MICROORGANISMS
MOLECULAR STRUCTURE
ORGANIC ACIDS
ORGANIC COMPOUNDS
PEPTIDES
PHOTOIONIZATION
PIGMENTS
POLYPEPTIDES
PROTEINS
RHODOPSIN
SYNTHESIS