Cation binding by bacteriorhodopsin
It was found that extensively washed purple membrane has about 1 calcium and 3-4 magnesium ions bound per bacteriorhodopsin molecule. When these divalent cations are removed by any of a variety of means, the pigment changes its color from purple to blue (lambda/sub max/ approx. = 600 nm). This blue pigment, which can be formed at near neutral pH, is probably very similar to blue species formed when the pH of a purple membrane sample is lowered to approx. = 2. When any of a wide variety of cations are added to a blue membrane preparation, the characteristic purple color of bacteriorhodopsin returns. Divalent and trivalent cations are much more efficient than monovalent cations in restoring the purple color and are effective at a ratio approaching one cation per pigment molecule. Besides shifting the absorption spectrum, removal of the divalent cations drastically alters the photochemical cycle of bacteriorhodopsin, including abolishing the unprotonated Schiff base (M-type) intermediate. Finally, lanthanum not only displaces the divalent cations normally bound to the purple membrane but also greatly reduces both the rate of decay of the M412 intermediate and proton uptake.
- Research Organization:
- Univ. of Illinois, Urbana
- DOE Contract Number:
- AC02-82ER12087
- OSTI ID:
- 5836796
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 82:2; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ALKALINE EARTH METALS
BINDING ENERGY
BIOCHEMICAL REACTION KINETICS
CALCIUM
CATIONS
CHARGED PARTICLES
CHARGED-PARTICLE TRANSPORT
CHEMICAL BONDS
CHEMICAL REACTIONS
ELEMENTS
ENERGY
IMINES
IONS
KINETICS
LANTHANUM
MAGNESIUM
METALS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PH VALUE
PHOTOCHEMICAL REACTIONS
PHOTOSYNTHETIC BACTERIA
PIGMENTS
PROTEINS
PROTON TRANSPORT
RADIATION TRANSPORT
RARE EARTHS
REACTION KINETICS
RHODOPSIN
SCHIFF BASES