Транспорт электронов в биологических системах - Рубин А.Б.
Скачать (прямая ссылка):
Feher G., Isacson R. A., McElroy J. D. et al. On the question of the primary acceptor in bacterial photosynthesis: Manganese substituting for iron in reaction centers of Rhodopseudomonas sphaeroides R-26.— Biochim Biophys. Acta, 1974, vol. 368, p. 135—139.
Feher G., Okamura M. Y. Reaction centers from Rhodopseudomonas sphaeroides.— Brookhaven Symp. Biol., 1977, vol. 28, p. 183—228.
Feher G., Okamura M. Y. Chemical composition and properties of reaction centers.— In: The Photosynthetic Bacteria/Ed. R. K. Clayton, W. R Sistrom. N. Y.: Plenum Press, 1978, p. 349—386.
Francis G. A., Richards W. Localization of photosynthetic membrane components in Rhodopseudomonas sphaeroides by a radioactive labeling procedure.—Biochemistry, 1980, vol. 19, p. 5104—5111.
Frey T. G., Chen S. 11. P., Schatz G. Structure and orientation of cytochrome с oxidase in crystalline membrane.— J. Biol. Chem., 1978, vol. 253, N12, p. 4389—4395.
Fuller S. D., Capaldi R. A., Henderson R. Structure of cytochrome с oxidase in deoxycholate-derived two-dimensional crystals.— J. Mol. Biol., 1979, vol. 134, p. 305—327.
Hales В. Temperature dependency of the rate of electron transport as a monitor of protein motion.—Biophys. J, 1976, vol. 16, p. 471—480.
Hales B., Gupta A. D. Orientation of the bacteriochlorophyll triplet and the primary ubiquinone acceptor of Rhodospirillum rubrum in membrane multilayers determined by ESR speclroscopy.—Biochim. Biophys. Acta, 1979, vol. 548, p. 276—286.
Hall R. E., Doorley P. F., Niedennan R. A. Transmembrane localization of reaction center proteins in Rhodopseudomonas sphaeroides chromatophores.— Photochem. and Photobiol, 1978, vol. 28, p. 273—276.
Haisey Ya. D., Parson W. W. Identification of ubiquinone as the secondary electron acceptor in the photosynthetic apparatus of Chromatium vinosum.— Biochim. Biophys. Acta, 1974, vol. 347, p. 404—416.
Hartnon H. J., Hall J. D., Crane F. L. Structure of mitochondrial cristae membranes.—Biochim. Biophys. Acta, 1974, vol. 344, p. 119—155. Harold F. M. Membranes and energy trunsduction in bacteria.— In: Current topics in bioenergetics/Ed. D. R. Sanadi. N. Y. etc.: Acad. Press, 1977, vol. 6, p. 83—149.
Hatch M. D., Boardman N. K. The biochemistry of plants. Photosynthesis/N. Y. etc.: Acad. Press, vol. 8,1981.
Hatefl Y., Galante Y. M. Organization of the mitochondrial respiratory chain.— In: Energy conservation in biological membranes/Ed. G. Schafer, M. Klingenberg. B. etc.: Spring. -Verlag, 1978, p. 19—30.
Ла1ф Y., Haavik A. G., Fowler E. R, Grilfilhs D. E. Studies on electron transfer System: Reconstitution of the electron transfer system.— J. Biol. Chem, 1962, vol. 237, p. 2661— 2669.
Hauska G. Transmembrane charge separation within the large subunit of photosystem I reaction centers from chloroplasts.—FEES Lett, 1980, vol. 119, p. 232—234.
Hauska G., Samoray D., Oiiich G., Nelson N. Reconstitution of photosynthetic energy conservation. П. Photophosphorylation in liposomes containing photosystem I reaction center and chloroplast coupling-factor complex.— Europ. J. Biochem, 1980, vol. П1, p. 535—543.
Hauska G., Trebsl A. Proton translocation in chloroplasts.— In: Current topics in bioenergetics/Ed. D. R. Sanadi. N. Y. etc.: Acad. Press, 1977, vol. 6, p. 151—220.
Heathcote P., Williams-Smith D. E., Sihra С. K., Evans М. C. W. The role of the membrane-bound iron-sulphur centers A and В in the photosystem I reaction centre of spinach chloroplasts.—Biochim. Biophys. Acta, 1978, vol. 503, p. 333—342.
Henderson R, Capaldi R A., Leigh J. S. Arrangement of cytochrome oxidase molecules in two-dimensional vesicle crystals.— J. Mol. Biol, 1977, vol. 112, p. 631—648.
Heron C., Ragan C. L, Trumpower B. L. The interaction between mitochondrial NADH-ubiquinone oxidoreductase und ubiquinol-cytochrome с oxidoreductase.—Biochem. J,
1978, vol. 174, p. 791—800.
Hill Т. E. Steady-state kinetic formalism applied to multienzyme complexes, oxidative phosphorylation and interacting enzymes.— Proc. Nat. Acad. Sci. US, 1976, vol. 73, N 12, p. 4432—4436.
Hill Т. E., Chance B. Steady-state kinetics of models of respiratory chain enzymes with isopotential pools and conformational site enzymes.— J. Thcor. Biol, 1978, vol. 72, N 1, p. 17—56.
Hinkle P. C. Coupling ratios of proton transport by mitochondria.— In: Chemiosmotic proton circuits in biological membranes/Ed. V. P. Skulachev, P. C. Hinkle. L. etc:: Addison-Wesley Publ. Co, 1981, p. 49—58.
Hinkle P. C., Kim J. J., Rocker E. Ion transport and respiratory control in vesicles formed from cytochrome oxidase and phospholipids.— J. Biol. Chem, 1972, vol. 247, N 4, p. 1338— 1339.
Hinkle P., Mitchell P. Effect of membrane potential on equilibrium poise between cytochrome a and cytochrome с in rat liver mitochondria.— J. Bioenerg, 1970, vol. 1, p. 45—60.
Holten D., Hoganson С., Windsor M. et al. Subpicosecond and picosecond studies of electron
transfer intermediates in Rhodopseudomonas sphaeroides reaction centers.— Biochim. Biophys. Acta, 1980, vol. 592, p. 461 —477.
