Charge recombination at low temperature in photosynthetic bacteria reaction centers: Evidence for two conformation states

[1]  Robert Eugene Blankenship,et al.  Formation and decay of radical-pair state P+I− in Chloroflexus aurantiacus reaction centers , 1986 .

[2]  W. W. Parson,et al.  Picosecond kinetics of the initial photochemical electron-transfer reaction in bacterial photosynthetic reaction centers. , 1985, Biochemistry.

[3]  C. Kirmaier,et al.  Photochemistry and electron transfer in borohydride-treated photosynthetic reaction centers , 1985 .

[4]  W. W. Parson,et al.  Temperature and detection-wavelength dependence of the picosecond electron-transfer kinetics measured in Rhodopseudomonas sphaeroides reaction centers. Resolution of new spectral and kinetic components in the primary charge-separation process , 1985 .

[5]  G. Feher,et al.  LM complex of reaction centers from Rhodopseudomonas sphaeroides R-26: characterization and reconstitution with the H subunit , 1985 .

[6]  W. W. Parson,et al.  Nanosecond fluorescence from isolated photosynthetic reaction centers of Rhodopseudomonas sphaeroides. , 1984, Biochimica et biophysica acta.

[7]  D. Kleinfeld,et al.  Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: evidence for light-induced structural changes. , 1984, Biochemistry.

[8]  A. Rutherford,et al.  A new EPR signal attributed to the primary plastosemiquinone acceptor in Photosystem II , 1984 .

[9]  Robert C. Davis,et al.  Relative enrichment of P-870 in photosynthetic reaction centers treated with sodium borohydride , 1984 .

[10]  G. Gingras,et al.  Different temperature dependencies of the charge recombination reaction in photoreaction centers isolated from different bacterial species , 1983 .

[11]  A. Verméglio,et al.  Structure of Rhodopseudomonas viridis reaction centers. Absorption and photoselection at low temperature , 1982 .

[12]  J. Jortner.  Dynamics of electron transfer in bacterial photosynthesis. , 1980, Biochimica et biophysica acta.

[13]  W. W. Parson,et al.  Subpicosecond and picosecond studies of electron transfer intermediates in Rhodopseudomonas sphaeroides reaction centers. , 1980, Biochimica et biophysica acta.

[14]  P. Avouris,et al.  Picosecond dynamics of primary electron-transfer processes in bacterial photosynthesis. , 1978, Biophysical journal.

[15]  V. Shuvalov,et al.  Picosecond detection of BChl‐800 as an intermediate electron carrier between selectively‐excited P 870 and bacteriopheophytin in Rhodospirillum rubrum relaction centers , 1978, FEBS letters.

[16]  A. Verméglio.  Secondary electron transfer in reaction centers of Rhodopseudomonas sphaeroides. Out-of-phase periodicity of two for the formation of ubisemiquinone and fully reduced ubiquinone. , 1977, Biochimica et biophysica acta.

[17]  P. Dutton,et al.  Picosecond Kinetics of Events Leading to Reaction Center Bacteriochlorophyll Oxidation , 1975, Science.

[18]  F. Reiss-Husson,et al.  Comparative studies on two reaction center preparations from Rhodopseudomonas speheroides Y , 1974, FEBS letters.

[19]  G. Feher,et al.  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. , 1974, Biochimica et biophysica acta.

[20]  C. Wraight,et al.  The absolute quantum efficiency of bacteriochlorophyll photooxidation in reaction centres of Rhodopseudomonas spheroides. , 1974, Biochimica et biophysica acta.

[21]  H. Yau,et al.  Photochemical electron transport in photosynthetic reaction centers from Rhodopseudomonas spheroides. I. Kinetics of the oxidation and reduction of P-870 as affected by external factors. , 1972, Biophysical journal.

[22]  E. Z. Szuts,et al.  Photochemical electron transport oin photosynthetic reaction centers from Rhodopseudomonas spheroides. 3. Effects of orthophenanthroline and other chemicals. , 1972, Biophysical journal.

[23]  W. W. Parson,et al.  In Chromatium, a single photochemical reaction center oxidizes both cytochrome C552 and cytochrome C555. , 1970, Biochimica et biophysica acta.