Deprotonation of lipid-depleted bacteriorhodopsin

Journal Article · Mon Aug 01 00:00:00 EDT 1988 · Proceedings of the National Academy of Sciences of the United States of America; (USA)

DOI:https://doi.org/10.1073/pnas.85.16.5918· OSTI ID:5518490

Jang, Dujeon; El-Sayed, M A ^[1]

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1. Univ. of California, Los Angeles (USA)

The removal of 75% of the lipid from bacteriorhodopsin caused the following: (i) decreased efficiency and rate of deprotonation of the protonated Schiff base (as monitored by absorption of the M{sub 412} intermediate); (ii) increased efficiency of deprotonation of deionized samples; (iii) a decrease by 1 unit in the pH at which deprotonation ceases; (iv) increased intensity of Eu{sup 3+} emission in Eu{sup 3+}-regenerated deionized delipidated samples; (v) increased exposure of the Eu{sup 3+} sites to water; and (vi) elimination of the dependence of the deprotonation efficiency on the metal cation concentration. These results are discussed in terms of changes in the protein conformation upon delipidation, which in turn control the deprotonation mechanism.

• DOE Contract Number: FG03-88ER13828
• OSTI ID: 5518490
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 85:16; ISSN 0027-8424; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ABSORPTION SPECTROSCOPY
BARYONS
BIOCHEMICAL REACTION KINETICS
CATIONS
CHARGED PARTICLES
CONFORMATIONAL CHANGES
ELEMENTARY PARTICLES
ELEMENTS
EUROPIUM COMPOUNDS
FERMIONS
HADRONS
IMINES
IONS
KINETICS
LIPIDS
MEMBRANES
METALS
NUCLEONS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PH VALUE
PHOTOSYNTHETIC BACTERIA
PHOTOSYNTHETIC MEMBRANES
PIGMENTS
PROTEINS
PROTONS
RARE EARTH COMPOUNDS
REACTION KINETICS
RHODOPSIN
SCHIFF BASES
SPECTROSCOPY
VITAMIN A
VITAMINS