Kinetic Isotope Effects in the Photochemical Cycle of Bacteriorhodopsin

Overview

Journal Biophys Struct Mech

Specialty Biophysics

Date 1976 Dec 22

PMID 1016693

Citations 13

Authors

R Korenstein

W V Sherman

S R Caplan

Affiliations

Soon will be listed here.

Abstract

Kinetics were determined for the four transients K590, L540, M410, O660 of the photochemical cycle of bacteriorhodopsin (BR570) both in 1H2O and in 2H2O over a wide temperature range. Breaks in the Arrhenius plots, observed at 25 degrees-32 degrees for the longest-lived transients coincide with a transition point in the microviscosity of the membrane as measured by depolarization of an added fluorescent probe. The earliest isotope effect occurs in the decay of L540, and is present in the subsequent formation and decay of M410 and O660. Thus in the light-driven proton pump of BR570, proton ejection from the Schiff base correlates with decay of L540 and reprotonation occurs with the decay of both M410 and O660 back to BR570.

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References

Teichberg V, Shinitzky M . Fluorescence polarization studies of lysozyme and lysozyme-saccharide complexes. J Mol Biol. 1973; 74(4):519-31. DOI: 10.1016/0022-2836(73)90044-2. View

Shinitzky M, Inbar M . Difference in microviscosity induced by different cholesterol levels in the surface membrane lipid layer of normal lymphocytes and malignant lymphoma cells. J Mol Biol. 1974; 85(4):603-15. DOI: 10.1016/0022-2836(74)90318-0. View

Lozier R, Bogomolni R, Stoeckenius W . Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium. Biophys J. 1975; 15(9):955-62. PMC: 1334761. DOI: 10.1016/S0006-3495(75)85875-9. View

Cogan U, Shinitzky M, Weber G, Nishida T . Microviscosity and order in the hydrocarbon region of phospholipid and phospholipid-cholesterol dispersions determined with fluorescent probes. Biochemistry. 1973; 12(3):521-8. DOI: 10.1021/bi00727a026. View

Lanyi J . Irregular bilayer structure in vesicles prepared from Halobactbrium cutirubrum lipids. Biochim Biophys Acta. 1974; 356(3):245-56. DOI: 10.1016/0005-2736(74)90265-x. View

Shinitzky M, Inbar M . Microviscosity parameters and protein mobility in biological membranes. Biochim Biophys Acta. 1976; 433(1):133-49. DOI: 10.1016/0005-2736(76)90183-8. View

Chu Kung M, Devault D, Hess B, Oesterhelt D . Photolysis of bacterial rhodopsin. Biophys J. 1975; 15(9):907-11. PMC: 1334750. DOI: 10.1016/S0006-3495(75)85864-4. View

Chance B, Porte M, Hess B, Oesterhelt D . Low temperature kinetics of H+ changes of bacterial rhodopsin. Biophys J. 1975; 15(9):913-7. PMC: 1334751. DOI: 10.1016/S0006-3495(75)85865-6. View

Dencher N, Wilms M . Flash photometric experiments on the photochemical cycle of bacteriorhodopsin. Biophys Struct Mech. 1975; 1(3):259-71. DOI: 10.1007/BF00535760. View

10.

Lewis A, Spoonhower J, Bogomolni R, Lozier R, Stoeckenius W . Tunable laser resonance raman spectroscopy of bacteriorhodopsin. Proc Natl Acad Sci U S A. 1974; 71(11):4462-6. PMC: 433906. DOI: 10.1073/pnas.71.11.4462. View

11.

Oesterhelt D, Stoeckenius W . Functions of a new photoreceptor membrane. Proc Natl Acad Sci U S A. 1973; 70(10):2853-7. PMC: 427124. DOI: 10.1073/pnas.70.10.2853. View

12.

Chignell C, Chignell D . A spin label study of purple membranes from Halobacterium halobium. Biochem Biophys Res Commun. 1975; 62(1):136-43. DOI: 10.1016/s0006-291x(75)80415-3. View

13.

Bridgen J, Walker I . Photoreceptor protein from the purple membrane of Halobacterium halobium. Molecular weight and retinal binding site. Biochemistry. 1976; 15(4):792-8. DOI: 10.1021/bi00649a010. View

14.

Weber G . Rotational Brownian motion and polarization of the fluorescence of solutions. Adv Protein Chem. 1953; 8:415-59. DOI: 10.1016/s0065-3233(08)60096-0. View

15.

Azzi A . The application of fluorescent probes in membrane studies. Q Rev Biophys. 1975; 8(2):237-316. DOI: 10.1017/s0033583500001803. View

16.

Sherman W, Korenstein R, Caplan S . Energetics and chronology of phototransients in the light response of the purple membrane of Halobacterium halobium. Biochim Biophys Acta. 1976; 430(3):454-8. DOI: 10.1016/0005-2728(76)90021-9. View

17.

Oesterhelt D, Stoeckenius W . Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat New Biol. 1971; 233(39):149-52. DOI: 10.1038/newbio233149a0. View

18.

Oesterhelt D, Meentzen M, Schuhmann L . Reversible dissociation of the purple complex in bacteriorhodopsin and identification of 13-cis and all-trans-retinal as its chromophores. Eur J Biochem. 1973; 40(2):453-63. DOI: 10.1111/j.1432-1033.1973.tb03214.x. View

19.

Sherman W, Slifkin M, Caplan S . Kinetic studies of phototransients in bacteriorhodopsin. Biochim Biophys Acta. 1976; 423(2):238-48. DOI: 10.1016/0005-2728(76)90182-1. View

20.

Mendelsohn R, Verma A, Bernstein H, Kates M . Structural studies of bacteriorhodopsin from Halobacterium cutirubrum by resonance Raman spectroscopy. Can J Biochem. 1974; 52(9):774-81. DOI: 10.1139/o74-110. View