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• W2567763721 abstract "Respiratory Complex I from E. coli may exist in two interconverting forms: resting (R) and active (A). The R/A transition of purified, solubilized Complex I occurring upon turnover was studied employing two different fluorescent probes, Annine 6+, and NDB-acetogenin. NADH-induced fluorescent changes of both dyes bound to solubilized Complex I from E. coli were characterized as a function of the protein:dye ratio, temperature, ubiquinone redox state and the enzyme activity. Analysis of this data combined with time-resolved optical measurements of Complex I activity and spectral changes indicated two ubiquinone-binding sites; a possibility of reduction of the tightly-bound quinone in the resting state and reduction of the loosely-bound quinone in the active state is discussed. The results also indicate that upon the activation Complex I undergoes conformational changes which can be mapped to the junction of the hydrophilic and membrane domains in the region of the assumed acetogenin-binding site." @default.
• W2567763721 created "2017-01-13" @default.
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• W2567763721 date "2017-01-01" @default.
• W2567763721 modified "2023-09-26" @default.
• W2567763721 title "Activation of respiratory Complex I from Escherichia coli studied by fluorescent probes" @default.
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• W2567763721 doi "https://doi.org/10.1016/j.heliyon.2016.e00224" @default.
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