[The temperature dependence of high-resolution 1H NMR spectra of Rhodobacter sphaeroides photosynthetic reaction centres in a temperature range of 25-40 degrees C].
High-resolution 1H-NMR spectra registered within a temperature range of 25-40 degrees C revealed a nonmonotonous dome-shaped temperature dependence of the ratio between integral NMR signal intensities determined at ppm intervals 2.5-4.5 and 0.2-2.5 with a maximum at 30 degrees C. This may be due to RC structural changes accompanying the temperature rise and accelerating the recombination reaction between oxidized bacteriochlorophyll and reduced primary quinone at temperatures above 30 degrees C.
Timofeev
V P
VP
Knox
P P
PP
Zakharova
N I
NI
Seĭfullina
N Kh
NKh
Rubin
A B
AB
D004579:Electron Transport; D006859:Hydrogen; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D012242:Rhodobacter sphaeroides / Q000378:metabolism*; D013696:Temperature
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D006859:Hydrogen