Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Eur Biophys J ; 36(6): 601-8, 2007 Jul.
Article in English | MEDLINE | ID: mdl-17262223

ABSTRACT

Laser-induced temperature jump experiments were used for testing the rates of thermoinduced conformational transitions of reaction center (RC) complexes in chromatophores of Chromatium minutissimum. The thermoinduced transition of the macromolecular RC complex to a state providing effective electron transport from the multiheme cytochrome c to the photoactive bacteriochlorophyll dimer within the temperature range 220-280 K accounts for tens of seconds with activation energy 0.166 eV/molecule. The rate of the thermoinduced transition in the cytochrome-RC complex was found to be three orders of magnitude slower than the rate of similar thermoinduced transition of the electron transfer reaction from the primary to secondary quinone acceptors studied in the preceding work (Chamorovsky et al. in Eur Biophys J 32:537-543, 2003). Parameters of thermoinduced activation of the electron transfer from the multiheme cytochrome c to the photoactive bacteriochlorophyll dimer are discussed in terms of cytochrome c docking onto the RC.


Subject(s)
Bacteriochlorophylls/physiology , Chromatium/physiology , Cytochromes c/physiology , Lasers , Photosynthetic Reaction Center Complex Proteins/physiology , Dimerization , Electron Transport , Temperature
2.
Eur Biophys J ; 32(6): 537-43, 2003 Sep.
Article in English | MEDLINE | ID: mdl-12679860

ABSTRACT

Methods of laser-induced temperature jumps and fast freezing were used for testing the rates of thermoinduced conformational transitions of reaction center (RC) complexes in chromatophores and isolated RC preparations of various photosynthesizing purple bacteria. An electron transfer reaction from primary to secondary quinone acceptors was used as a probe of electron transport efficiency. The thermoinduced transition of the acceptor complex to the conformational state facilitating electron transfer to the secondary quinone acceptor was studied. To investigate the dynamics of spontaneous decay of the RC state induced by the thermal pulse, the thermal pulse was applied either before or during photoinduced activation of electron transport reactions in the RC acceptor complex. The maximum effect was observed if the thermal pulse was applied against the background of steady-state photoactivation of the RC. It was shown that neither the characteristic time of the thermoinduced transition within the temperature range 233-253 K nor the characteristic time of spontaneous decay of this state at 253 K exceeded several tens of milliseconds. Independent support of the estimates was obtained from experiments with varied cooling rates of the samples tested.


Subject(s)
Benzoquinones/metabolism , Electron Transport/radiation effects , Freezing , Hot Temperature , Photosynthetic Reaction Center Complex Proteins/metabolism , Photosynthetic Reaction Center Complex Proteins/radiation effects , Adaptation, Physiological/radiation effects , Benzoquinones/radiation effects , Cells, Cultured , Dose-Response Relationship, Radiation , Light , Photosynthetic Reaction Center Complex Proteins/chemistry , Protein Conformation/radiation effects , Radiation Dosage , Rhodobacter sphaeroides/metabolism , Rhodobacter sphaeroides/radiation effects , Rhodospirillum rubrum/metabolism , Rhodospirillum rubrum/radiation effects , Structure-Activity Relationship , Temperature
SELECTION OF CITATIONS
SEARCH DETAIL
...