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Updated: Aug 2, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Effect of monochromatic UV-B radiation on electron transfer reactions of Photosystem II
A W Larkum1, M Karge, F Reifarth
1School of Biological Sciences, University of Sydney, NSW, 2006, Australia.
Abstract:
The adverse effect of low intensity, small band UV-B irradiation (lambda = 305 +/- 5 nm, I = 300 mW m(-2)) on PS II has been studied by comparative measurements of laser flash-induced changes of the absorption at 325 nm, DeltaA(325)(t), as an indicator of redox changes in Q(A), and of the relative fluorescence quantum yield, F(t)/F(o), in PS II membrane fragments. The properties of untreated control were compared with those of samples where the oxygen evolution rate under illumination with continuous saturating light was inhibited by up to 95%. The following results were obtained: a) the detectable initial amplitude (at a time resolution of 30 mus) of the 325 nm absorption changes, DeltaA(325), remained virtually invariant whereas the relaxation kinetics exhibit significant changes, b) the 300 mus kinetics of DeltaA(325) dominating the relaxation in UV-B treated samples was largely replaced by a 1.3 ms kinetics after addition of MnCl(2), c) the extent of the flash induced rise of the relative fluorescence quantum yield was severely diminished in UV-B treated PS II membrane fragments but the relaxation kinetics remain virtually unaffected. Based on these results the water oxidizing complex (WOC) is inferred to be the primary target of UV-B impairment of PS II while the formation of the 'stable' radical pair P680(+*)Q(A) (-) (*) is almost invariant to this UV-B treatment.
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