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- W2959698949 abstract "ABSTRACT Fluorescent signals associated with Complex I (NADH:ubiquinone oxidoreductase type I) upon its reduction by NADH without added acceptors and upon NADH:ubiquinone oxidoreduction were studied. Two Complex I-associated redox-dependent signals were observed: with maximum emission at 400 nm (λex = 320 nm) and 526 nm (λex = 450 nm). The 400 nm signal derived from ubiquinol accumulated in Complex I/DDM (n-dodecyl β-D-maltopyranoside) micelles. The 526 nm redox signal unexpectedly derives mainly from FMN (flavin mononucleotide), whose fluorescence in oxidized protein is fully quenched, but arises transiently upon reduction of Complex I by NADH. The paradoxical flare-up of FMN fluorescence is discussed in terms of conformational changes in the catalytic site upon NADH binding. The difficulties in revealing semiquinone fluorescent signal are considered." @default.
- W2959698949 created "2019-07-23" @default.
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- W2959698949 date "2019-06-01" @default.
- W2959698949 modified "2023-09-24" @default.
- W2959698949 title "Fluorescent signals associated with respiratory Complex I revealed conformational changes in the catalytic site" @default.
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- W2959698949 doi "https://doi.org/10.1093/femsle/fnz155" @default.
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