[Electron paramagnetic resonance of the F1-H+-ATPase complex and adenosine triphosphate synthesis after its irradiation with visible light].

Under F1-ATPase irradiation by visible light two characteristic features of flavin main activities were detected: I/ESR signal g = 2.00 appearance which was in favor of flavin photochemical electron reduction and 2/photostimulated O2 consumption by F1-ATPase. The dependence of ESR signal g = 2.00 intensity on visible light wavelength completely coincided with the same dependence obtained for proteinless model riboflavin + ADP. Flavin localization in proximity of ADP bound in the enzyme active site was suggested. Under F1-ATPase irradiation by light lambda greater than 350 nm ATP synthesis was obtained similar to the proteinless model riboflavin + ADP + Pinorg. In this model endogenous flavin was suggested to serve as a photosensitizer, its photoexcitement being a model of dark energization of F1-ATPase in oxidative phosphorylation.