Bluelight-induced, flavin-mediated transport of redox equivalents across artificial bilayer membranes.
This paper continues our studies of physico-chemical properties of vesicle-bound flavins. Based on previous results, an advanced model system was designed in order to study the mechanisms underlying bluelight-induced redox transport across artificial membranes. The lumen of single-shelled vesicles was charged with cytochrome c, and amphiphilic flavin (AF1 3, AF1 10) was bound to the membrane. Upon bluelight irradiation redox equivalents are translocated from exogeneous 1e-(EDTA)-and 2e-(BH3CN-) donors across the membrane finally reducing the trapped cytochrome c both under aerobic and anaerobic conditions. The mechanisms involved are explored and evidence for the involvement of various redox states of oxygen, dihydroflavin and flavosemiquinone is presented.
D001692:Biological Transport; D003574:Cytochrome c Group; D004492:Edetic Acid / Q000378:metabolism; D005415:Flavins / Q000502:physiology*; D008027:Light; D008051:Lipid Bilayers; D010084:Oxidation-Reduction; D010100:Oxygen / Q000502:physiology; D010786:Photoreceptor Cells / Q000502:physiology* / Q000528:radiation effects; D013481:Superoxides / Q000502:physiology
D003574:Cytochrome c Group; D005415:Flavins; D008051:Lipid Bilayers; D013481:Superoxides; D004492:Edetic Acid; D010100:Oxygen