Role of carboxyl residues and membrane lipids in cation binding to bacteriorhodopsin.
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.
Hrabeta-Robinson
E
E
Applied Science Division, Lawrence Berkeley Laboratory, University of California, Berkeley 94720.
Semadeni
M
M
Packer
L
L
D001436:Bacteriorhodopsins / Q000378:metabolism*; D002412:Cations; D002712:Chlorides; D004492:Edetic Acid; D006217:Halobacterium / Q000378:metabolism*; D008345:Manganese / Q000378:metabolism; D017895:Manganese Compounds; D008563:Membrane Lipids / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry
D002412:Cations; D002712:Chlorides; D017895:Manganese Compounds; D008563:Membrane Lipids; D008345:Manganese; D001436:Bacteriorhodopsins; D004492:Edetic Acid; C025340:manganese chloride