Транспорт электронов в биологических системах - Рубин А.Б.
Скачать (прямая ссылка):
Hinkle P. С., Kim J. J., Racker 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., Hogans on C., 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.
Holzapfel G., Bauer R. Computer simulation of primary photosynthetic reactions compared with experimental result on C>2 exchange and chlorophyll fluorescence of green plants.—Zlschr. Naturforsch., 1975, Bd. 30, S. 489—498.
Hurt K, Hauska G. A cytochrome f7bc complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts.— Europ. J. Biochem.. 1981, vol. 117, p. 591—599.
Hurt K, Hauska G. Involvement of plastoquinone bound within the isolated cytochrome b6-f complex from chloroplasts in oxidant-induced reduction of cytochrome b6.— Biochim. Biophys. Acta, 1982, vol. 682, p. 466—473.
Ingledew W. J., Ohnishi I An analysis of some thermodynamic properties of iron-sulphur centers in site I of mitochondria.— Biochem. J., 1980, vol. 186, p. Ill — 117.
Iloh S. Effects of surface potential and membrane potential on the midpoint potential of cylochrome c-555 bound to the chromatophore membrane of Chromatium vinosum.— Biochim. Biophys. Acta, 1980, vol. 591, p. 346— 355.
Izawa S., Good N. E. Effect of salt and electron transport on the conformation of isolated chloroplasts. II. Electron microscopy.— Plant Physiol., 1966, vol. 41, p. 544—552.
Jackson J. B., Button P. L. The kinetic and redox potentiometric resolution of the carotenoid shifts in Rhodopseudomonas sphaeroides chromatophores: Their relationship to electric field alterations in electron transport and energy coupling.—Biochim. Biophys. Acta, 1973, vol. 325, p. 102—113.
Johansson В. C., Baltscheffsky M. On the subunit composition of the coupling factor (ATP ase) from Rhodospirillum rubrum.—FEES Lett., 1975, vol. 53,. p. 221—224.
Jolchine G., Reiss-Husson F. Studies on pigments and lipids in Rhodopseudomonas sphaeroides Y reaction center.— FEBS Lett., 1975, vol. 52, p. 33—36.
Kadenbach B., Merle P. On the function of multiple subunits of cytochrome с oxidase from higher eukaryotes.— FEBS Lett., 1981, vol. 131, N 1, p. I —11..
Kagawa Y. Energy-transducing proteins in thermophilic biomembranes.— J. Membrane Biol.,
1980, vol. 55, p. 1—8.
Kakuno Т., Barlsch R C., Nlshikawa K, Horio T. Redox components associated with chromatophores from Rhodospirillum rubrum G-9.— J. Biochem., 1971, vol. 70, p. 79— 94,
Kaufman K. J., Dution P. L., Netzel T. L. et al. Picosecond kinetics of events, leading to reaction centers bacteriochlorophyll oxidation.— Science, 1975, vol. 188, p. 1301 — 1304.
Ke B. The primary electron acceptors in green-plant photosystem I and photosynthetic bacteria.— In: Current topics in bioenergetics/Ed. D. R. Sanadi, L. P. Vernon. N. Y. etc.: Acad. Press. 1978, p. 75—138.
Keilin D. The history of cell respiration and cytochromes. Cambridge: Univ. Press, 1966.
Kevin L., Wingfield P., Arad Т., Weiss H. Three-dimensional structure of ubiquinol: cytochrome с reductase from Neurospora mitochondria determined by electron microscopy of membrane crystals.— J. Mol. Biol., 1981, vol. 149, N 2, p. 259—274.
Kihara Т., Chance B. Cytochrome photooxidation at liquid nitrogen temperatures in photosynthetic bacteria.—Biochim. Biophys. Acta, 1969, vol. 189; p. 116—124.
King Т. K, Orii Y., Chance B., OkuniikiK, Cytochrome oxidase. Amsterdam etc.: Elsevier/North Holland Biomed. Press, 1979.
Klimov V. V., KlevanikA. V, Shuvalov V. A, Krasnov sky A. A. Reduction of pheophytin in the primary light reaction of photosystem II.— FEES Lett., 1977, vol. 82, p. 183—186.
Klimov V. V, Krasnovsky A. A. Pheophytin as the primary electron acceptor in photosystem II reaction centers.—Photosynthetica, 1981, vol. 15, p. 592—609.
King Т. К, Yu L., Yu С., Wei Y. Subunits of cytochrome oxidase and their large scale preparations.— In: Cytochrome oxidase/Ed. Т. E. King et al. Amsterdam etc.: Elsevier/Norlh Holland Biomed. Press, 1979, p. 53—65.
Knaff D. B. The primary reaction of plant photosystem II.— Photochem. and Photobiol., 1977, vol. 26, p. 327—340.
Knaff D. B. Reducing potentials and the pathway of NAD+ reduction.— In: The Photosynthetic Bacteria/Ed. R. K. Clayton, W. R. Sistrom. N. Y.: Plenum Press, 1978, p. 525—571.
Кок B. Light-induced absorption changes in photosynthetic organisms. II. A split-beam difference spectrophotometer.— Plant Physiol., 1959, vol 34, p. 184—192.
KokB., For bush B., McGloin M. Cooperation of charges in photosynthetic 02 evolution. 1. A linear four step mechanism.— Photochem. and Photobiol., 1970, vol. 11, p. 457—475.
