AbstractEPR signals due to c-type cytochromes in Rhodopseudomonas viridis reaction centres are reported. Haems with Em = 380 mV (1), 310 mV (1) and about 0 mV (2) were identified. At redox potentials where the low-potential cytochromes are oxidised, but the high-potential cytochromes are reduced, photooxidation of the high-potential cytochromes is observed as QA is photoreduced by low-temperature (15 K) illumination. Cyt c-556→cyt c-559→reaction centre→QA However, the signal attributed to QA is only 30–40% of the intensity and is narrower than that observed when QA photoreduced with all the haems reduced. It is suggested that reduction of the low-potential haems causes conformational changes in the reaction centre, altering the iron-quinone...
AbstractAbsorbance difference spectroscopy has been used to study electron transfer reactions at low...
AbstractGel-electrophoretic assay revealed that the photosynthetic reaction center (RC) of Chromatiu...
AbstractThe correlation between the reduction of QA and the oxidation of TyrZ or Car/ChlZ/Cytb559 in...
AbstractEPR signals due to c-type cytochromes in Rhodopseudomonas viridis reaction centres are repor...
AbstractThe kinetics of electron transfer from the third highest potential heme (c-522, Em = +20 mV)...
AbstractElectron transfer from the tetraheme cytochrome c to the special pair of bacteriochlorophyll...
AbstractThe photooxidation of c559, c556, and c552 hemes in Rhodopseudomonas viridis cytochrome has ...
Bacterium Rhodopseudomonas viridis has four c-type cytochromes integrated to a single protein subuni...
AbstractElectron transfer from the proximal heme c-559 to the primary donor P has been studied in re...
AbstractLow temperature absorption and linear dichroism measurements on oriented reaction centers of...
Photochemical reaction centers prepared from Rhodopseudomonas spheroides were treated with reduced c...
AbstractThe redox and spectral characteristics of the 4-heme cytochrome c unit of the photochemical ...
Cytochrome bd-I is one of the three proton motive force-generating quinol oxidases in the O2-depend...
AbstractThe electron transfer reactions from low-potential cytochrome c-551, high-potential iron-sul...
The structure of the photosynthetic reaction center (RC) from Rhodopseudomonas viridis is known to h...
AbstractAbsorbance difference spectroscopy has been used to study electron transfer reactions at low...
AbstractGel-electrophoretic assay revealed that the photosynthetic reaction center (RC) of Chromatiu...
AbstractThe correlation between the reduction of QA and the oxidation of TyrZ or Car/ChlZ/Cytb559 in...
AbstractEPR signals due to c-type cytochromes in Rhodopseudomonas viridis reaction centres are repor...
AbstractThe kinetics of electron transfer from the third highest potential heme (c-522, Em = +20 mV)...
AbstractElectron transfer from the tetraheme cytochrome c to the special pair of bacteriochlorophyll...
AbstractThe photooxidation of c559, c556, and c552 hemes in Rhodopseudomonas viridis cytochrome has ...
Bacterium Rhodopseudomonas viridis has four c-type cytochromes integrated to a single protein subuni...
AbstractElectron transfer from the proximal heme c-559 to the primary donor P has been studied in re...
AbstractLow temperature absorption and linear dichroism measurements on oriented reaction centers of...
Photochemical reaction centers prepared from Rhodopseudomonas spheroides were treated with reduced c...
AbstractThe redox and spectral characteristics of the 4-heme cytochrome c unit of the photochemical ...
Cytochrome bd-I is one of the three proton motive force-generating quinol oxidases in the O2-depend...
AbstractThe electron transfer reactions from low-potential cytochrome c-551, high-potential iron-sul...
The structure of the photosynthetic reaction center (RC) from Rhodopseudomonas viridis is known to h...
AbstractAbsorbance difference spectroscopy has been used to study electron transfer reactions at low...
AbstractGel-electrophoretic assay revealed that the photosynthetic reaction center (RC) of Chromatiu...
AbstractThe correlation between the reduction of QA and the oxidation of TyrZ or Car/ChlZ/Cytb559 in...