PMID: 2493216Mar 1, 1989Paper

Role of carboxyl residues and membrane lipids in cation binding to bacteriorhodopsin

Archives of Biochemistry and Biophysics
E Hrabeta-RobinsonL Packer

Abstract

To investigate the site specificity of cation binding to bacteriorhodopsin, carboxyl groups were chemically modified in purple membrane preparations from Halobacterium halobium. Cation binding followed by EPR and visible spectroscopy has led us to the conclusion that two cations bind to the surface regions and that at least one cation binds to carboxyl groups in the protein interior. Conformational freedom is necessary for the cooperative conversion of deionized blue species to cation-reconstituted purple species. Studies of white membranes from the JW-5 strain showed that a higher content of charged lipids results in the binding of approximately 100 more color-regulating cations and in negative cooperativity in the blue-to-purple species conversion. A greater dependence of protein structure on these bound cations suggests a role for cations in the modulation of opsin-lipid interaction.

References

Aug 1, 1986·Biophysical Journal·N V KatreR M Stroud
Jan 1, 1982·Annual Review of Biochemistry·W Stoeckenius, R A Bogomolni
Aug 16, 1984·Biochemical and Biophysical Research Communications·E HrabetaL Packer
Oct 30, 1984·Biochemical and Biophysical Research Communications·S Wu-ChouL Packer
Nov 1, 1984·Photochemistry and Photobiology·Y KimuraW Stoeckenius
Jul 18, 1984·Biochemical and Biophysical Research Communications·L PackerP Volfin
Mar 1, 1986·Biophysical Journal·C H ChangT G Ebrey

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Citations

Jan 1, 1991·Archives of Biochemistry and Biophysics·M E RivièreJ Faure

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