Abstract
Light generates a pH gradient and an electrical potential across the purple membrane of Halobacterium halobium. We are investigating the time resolved changes in protonation of the side chains of specific amino acid residues and the correlation of these changes with photon absorption and the ensuing photo-reaction cycle. We seek to determine the precise molecular description of the photocycle and of the time dependent steps in the uptake, translocation, and release of protons by the retinal proton catalyst in this membrane, bacteriorhodopsin (BR).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
W. Stoeckenius and R. Lozier, Light Energy Conversion in Halobacterium halobium, J. Supramol. Struct. 2: 769–774 (1974).
T. Konishi, S. Tristram and L. Packer, The Effect of Cross-linking on the Photocycing Activity of Bacteriorhodopsin, Photochem. Photobiol. 29: 353–358 (1979).
T. Konishi and L. Packer, Light-Dark Conformational States in Bacteriorhodopsin, Biochem. Biophys. Res. Commun. 72: 1437–1441 (1976).
L. Packer, S. Tristram, J. Herz, C. Russell and C. Borders, Chemical Modification of Purple Membranes: Role of Arginine and Carboxylic Acid Residues in Bacteriorhodopsin, FEBS Letts. 108: 243–248 (1979).
P. Scherrer, C. Carmeli, P. Shieh and L. Packer, The Effect of Chemical Modification of Tyrosyl Residues on Proton Conductivity Mediated by Bacteriorhodopsin, Biophys. J. 25: 207a (1979).
P. Scherrer, L. Packer, S. Seltzer and M. Lin, Involvement of Tyrosine Residues in Bacteriorhodopsin Activity, (submitted for publication).
R. Korenstein, W. Sherman and R. Caplan, Kinetic Isotope Effects in the Photochemical Cycle of Bacteriorhodopsin, Biophys. Struct. Mech. 2: 267–276 (1976).
P. Sullivan, A. Quintanilha, S. Tristram and L. Packer, Isotope Effects and Activation Parameters for Chemically Modified Bacteriorhodopsin, FEBS Letts. 117: 359–362 (1980).
R.J. Mehlhorn and L. Packer, Membrane Surface Potential Measurements with Amphiphilic Spin Labels, in: “Methods in Enzymology,” S. Fleischer and L. Packer, eds., Academic Press, New York, Vol. 56, pp. 515–527, (1979).
R.J. Mehlhorn, T. Racanelli and L. Packer, Simultaneous Measurements of Proton Movement and Membrane Potential Changes in the Wild Type and Mutant Halobacterium halobium Vesicles, in: “Methods in Enzymology,” L. Packer, ed., Academic Press, New York, Vol. 88, pp. 334–344 (1982).
R.J. Mehlhorn, P. Candau and L. Packer, Measurements of Electrochemical Gradients with Spin Probes, in: “Methods in Enzymology,” L. Packer, ed., Academic Press, NY, Vol. 88, pp. 761–762, (1982).
C. Carmeli, A. Quintanilha, and L. Packer, Light-Induced Surface Potential Changes in Purple Membranes and Bacteriorhodopsin Liposomes, in: “Membrane Bioenergetics,” C.P. Lee, G. Schatz, L. Ernster, eds., Addison Wesley Publishing Co., Reading, MA (1980).
C. Carmeli, A. Quintanilha, and L. Packer, Surface Charge Changes in Purple Membranes and the Photoreaction Cycle of Bacteriorhodopsin, PNAS, 77: 4707–4011 (1980).
A. Quintanilha, Control of the Photocycle in Bacteriorhodopsin by Electrochemical Gradients, FEBS Letts. 117: 8–12 (1980).
M. Camps-Cavieres, T. Moore and R. Perham, Effect of Modification of the Tyrosine Residues of Bacteriorhodopsin with Tetranitromethane, Biochem. J. 179: 233–238 (1979).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1985 Springer Science+Business Media New York
About this chapter
Cite this chapter
Packer, L., Quintanilha, A.T., Mehlhorn, R.J. (1985). Application of Chemical Modification and Spin Labeling Techniques to the Study of Energy Conversion by Bacteriorhodopsin. In: Pullman, A., Vasilescu, V., Packer, L. (eds) Water and Ions in Biological Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0424-9_52
Download citation
DOI: https://doi.org/10.1007/978-1-4899-0424-9_52
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-0426-3
Online ISBN: 978-1-4899-0424-9
eBook Packages: Springer Book Archive