Temperature dependence of the electrogenic reaction in the Q(B) site of the Rhodobacter sphaeroides photosynthetic reaction center: the Q(A)(-)Q(B)->Q(A)Q(B)(-) transition

Autor(en): Gopta, OA
Bloch, DA
Cherepanov, DA
Mulkidjanian, AY
Stichwörter: (Rhodobacter sphaeroides); BACTERIAL REACTION CENTERS; Biochemistry & Molecular Biology; Biophysics; Cell Biology; CHROMATOPHORES; DIFFERENCE SPECTROSCOPY; electrogenesis; electron transfer; MUTANTS; PATHWAY; photosynthetic reaction center; PROTEIN; proton transfer; PROTON-TRANSFER; purple photosynthetic bacterium; REDUCTION; SECONDARY QUINONE ACCEPTOR; ubiquinone
Erscheinungsdatum: 1997
Herausgeber: ELSEVIER SCIENCE BV
Enthalten in: FEBS LETTERS
Band: 412
Ausgabe: 3
Startseite: 490
Seitenende: 494
Zusammenfassung: 
The temperature dependencies for the kinetics and relative amplitudes of electrogenic reaction(s) coupled with the first reduction of the secondary quinone acceptor Q(B) were measured with dark-adapted chromatophores of Rhodobacter sphaeroides. The kinetics, while acceptable fitted by a single exponent at room temperature, clearly split into two components below 15 degrees C (rise times, 25 mu s and 300 mu s at pH 7.0 and 10 degrees C) with the slow phase ousting the fast one at pH>9.0, The activation energies of the fast and slow phases Here estimated at pH 7.0 as <10 kJ/mol and 60-70 kJ/mol, respectively, To explain the kinetic heterogeneity of the Q(B)-->Q(B)(-)transition, we suggest two possible conformations for the neutral oxidized ubiquinone at the QB site: one with a hydrogen bond between the side chain carboxyl of Glu-L212 and the methoxy oxygen at C-3 of the Q(B) ring (Q(B)-H-Glu centers) and the other one, without this bond (Q(B):Glu(-)centers), The fast phase is attributed to Q(A)(-)Q(B)-H-Glu-->Q(A)Q(B)-H-Glu transition, whereas the slow one to the Q(A)-Q(B):Glu(-)-->Q(A)(-)Q(B)-H-Glu-->Q(A)Q(B)(-)-H-Glu transition. (C) 1997 Federation of European Biochemical Societies.
ISSN: 00145793
DOI: 10.1016/S0014-5793(97)00842-9

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