Light energy conversion in Halobacterium halobium.

Halobacterium halobium carries out photophosphorylation. A rhodopsin-like protein, bacteriorhodopsin, located in the cell membrane mediates the first step in energy transduction, the conversion of light energy into a chemiosmotic gradient. After absorption of a photon, bacteriorhodopsin undergoes a series of fast reactions, returning to its original state in a few milliseconds. In continuous light it cycles continuously at 100 to 200 cps. During a cycle protons are taken up on the cytoplasmic side of the membrane and released on the outer surface, thus generating a chemiosmotic gradient which can drive phosphorylation of ADP to ATP.

[1]  W. Hubbell,et al.  Preparation and properties of phospholipid bilayers containing rhodopsin. , 1972, Proceedings of the National Academy of Sciences of the United States of America.

[2]  D. Oesterhelt,et al.  Functions of a new photoreceptor membrane. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[3]  W. Stoeckenius,et al.  FURTHER CHARACTERIZATION OF PARTICULATE FRACTIONS FROM LYSED CELL ENVELOPES OF HALOBACTERIUM HALOBIUM AND ISOLATION OF GAS VACUOLE MEMBRANES , 1968, The Journal of cell biology.

[4]  P. Mitchell Chemiosmotic coupling in energy transduction: A logical development of biochemical knowledge , 1972, Journal of bioenergetics.

[5]  D. Oesterhelt,et al.  Reversible dissociation of the purple complex in bacteriorhodopsin and identification of 13-cis and all-trans-retinal as its chromophores. , 1973, European journal of biochemistry.

[6]  T. Yoshizawa,et al.  The chemistry of visual photoreception. , 1965, Cold Spring Harbor symposia on quantitative biology.

[7]  W. Stoeckenius,et al.  Structure of the purple membrane. , 1971, Nature: New biology.

[8]  G. Wald,et al.  Photochemistry of Iodopsin , 1967, Nature.

[9]  W. Stoeckenius,et al.  Tunable laser resonance raman spectroscopy of bacteriorhodopsin. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[10]  W. Stoeckenius,et al.  Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation. , 1974, The Journal of biological chemistry.

[11]  D. Oesterhelt,et al.  Rhodopsin-like protein from the purple membrane of Halobacterium halobium. , 1971, Nature: New biology.

[12]  B. Hess,et al.  Reversible photolysis of the purple complex in the purple membrane of Halobacterium halobium. , 1973, European journal of biochemistry.

[13]  W. Stoeckenius,et al.  Photophosphorylation in Halobacterium halobium. , 1974, Proceedings of the National Academy of Sciences of the United States of America.