Транспорт электронов в биологических системах - Рубин А.Б.
Скачать (прямая ссылка):
Matsuura K.., Nishimura M. Diffusion-potential-induced oxidation and reduction of cytochromes in chromatophores from Rhodopseudomonas sphaeroides.— J. Biochem.,
1978, vol. 84, p. 539—546.
McCarty R E. The ATP-ase complex of chloroplasts and chromatophores.— In: Current topics in bioenergetics/Ed. D. R. Sanadi, L. P. Vernon. N. Y. etc.: Acad. Press, 1978, vol.
7, p. 245—278.
McCarty R E. Photosynthetic phosphorylation by chloroplasts of higher plants.— In: Photochemical and photobiological reviews/Ed. К. C. Smith. N. Y.; L.: Plenum Press,
1980, vol. 5, p. 1—47.
McElroy J. D., Mauzerall D. С., Feher G. Characterization of primary reactants in bacterial photosynthesis. II. Kinetic studies of the light-induced EPR signal (g-2.0026) and the optical absorbance changes at cryogenic temperatures.—Biochim. Biophys. Acta, 1974, vol. 333, p. 261—277.
Meinhard S. W., Crofts A. R. Kinetic and thermodynamic resolution of cytochrome Ci from Rhodopseudomonas sphaeroides.— FEBS Lett., 1982. vol. 149, p. 223—227.
Merli A., Capaldi R A., Ackrell В. A. C., Kearney E. B. Arrangement of complex II (succinate-ubiquinone reductase) in the mitochondrial inner membrane.—Biochemistry,
1979, vol. 18, N 8, p. 1393—1400.
Miller K. R, Staehelin L. A. Analysis of the thylakoid outer surface: Coupling factor is limited to unstacked membrane regions.— J. Cell Biol., 1976, vol. 68, p. 30—47.
Mitcliell P. Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism.— Nature, 1961, vol. 191, p. 144—148.
Mitchell P. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation.—Biol. Revs, 1966, vol. 41, p. 445—502.
Mitchell P. Protonmotive function of cytochrome systems.— In: Electron transfer chains and oxidative phosphorylation/Ed. E. Quagliariello et al. Amsterdam etc.: North Holland Publ. Co, 1975, p. 305—316.
Mitchell P. Possible molecular mechanisms of the protonmotive function of cytochrome systems.—J. Theor. Biol., 1976, vol. 62, p. 327—367.
Miiller H. W., Baltscheffsky M. On the oligomycin-sensitivity and subunit composition of the ATFase complex from Rhodospirillum rubrum.— Ztschr. Naturforsch., 1979, Bd. 31, S. 229—232.
Nuchushiai R., Nelson N Photosystem I reaction centers from Chlamydomonas and higher plant chloroplasts.— J. Bioenerg. and Biomembr., 1981, vol. 13, p. 295—306.
Nelson N, Neumann J, Isolation of a cytochrome b6-f particle from chloroplasts.—J. Biol. Chem., 1972, vol. 247, p. 1817—1824,
Nelzel T. L., Rentzepis P. М., Leigh J. Picosecond kinetics of reaction centers containing bacteriochlorophyll.— Science, 1973, vol. 182, p. 238—240.
Netzel I L., Rentzepis P. М., Tiede D. M. et al. Effect of reduction of reaction center intermediate upon the picosecond oxidation reaction of the bacteriochlorophyll dimer in Chromatium vinosum and Rhodopseudomonas viridis.— Biochim. Biophys. Acta, 1977, vol. 460, p. 467—479.
Nicolson P., Petersen L. G. Haem-haem interactions in cytochrome aa3 during the anaerobic-aerobic transition.— Biochim. Biophys. Acta, 1974, vol. 357, p. 462—467.
Nikolaev G. М., Knox P. P., Kononenko A. A. et al. Photo-induced electron transport and water state in Rhodospirillum rubrum chromatophores.— Biochim. Biophys. Acta, 1980, vol. 590, p. 194—201.
Nugent J. H A, Diner B. A, Evans М. C. W. Direct detection of the electron acceptor of photosystem II: Evidence that Q is an iron-quinone complex.— FEBS Lett, 1981a, vol. 124, p. 241—244.
Nugent J. H. A., Moller B. L., Evans М. C. W. Comparison of the EPR properties of photosystem I iron-sulphur centers A and В in spinach and barley.—Biochim. Biophys. Acta, 1981b, vol. 634, p. 249—255.
Odermalt E., Snozzi М., Bachojen R Labeling of chromatophore membranes and reaction centers from the photosynthetic bacterium Rhodospirillum rubrum with the hydrophobic marker 5-125I iodonaphtyl-l-azide.— Biochim. Biophys. Acta, 1980, vol. 591, p. 372—380.
Ohnishi T. Thermodynamic and EPR characterization of iron-sulfur centers in the NADH-ubiquinone segment of the mitochondrial respiratory chain in pigeon heart.— Biochim. Biophys. Acta, 1975, vol. 387, p. 475—490.
Ohnishi Т., Lim J., Winter B., King T. Thermodynamic and EPR characteristics of a HiPiP-type iron-sulfur center in the succinate dehydrogenase of the respiratory chain.—J. Biol. Chem., 1976a, vol. 251, N 7, p. 2105—2109.
Ohnishi Т., Salerno /. C., Winter D. B. et al. Thermodynamic and EPR characteristics of two ferredoxin-type iron-sulfur centers in the succinate-ubiquinone reductase segment of the respiratory chain.— J. Biol. Chem., 1976b, vol. 251, N 7, p. 2094—2104.
Ohnishi Т., Trumpower B. L. Different effects of antimycin on ubisemiquinone bound in different environments in isolated succinate cytochrome с reductase complex.—J. Biol. Chem., 1980, vol. 255, N 8, p. 3278—3284.
Okamura M. Y., Isaacson R A, Feher G. Primary acceptor in bacterial photosynthesis: Obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas sphaeroides.— Proc. Nat. Acad. Sci. US, 1975, vol. 72, p. 3491—3495.
