[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.
Nedelina
O S
OS
Brzhevskaia
O N
ON
Lozinova
T A
TA
Kaiushin
L P
LP
D000255:Adenosine Triphosphate / Q000096:biosynthesis* / Q000528:radiation effects; D004578:Electron Spin Resonance Spectroscopy; D008027:Light; D010084:Oxidation-Reduction; D010777:Photochemistry; D006180:Proton-Translocating ATPases / Q000032:analysis / Q000528:radiation effects*
D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases
Elektronnyĭ paramagnitnyĭ rezonans kompleksa F1-H+-ATPazy i sintez adenozintrifosfata pri ego osveshchenii vidimym svetom.