PMID:15137097

Citation	Hellwig, P, Stolpe, S and Friedrich, T Fourier transform infrared spectroscopic study on the conformational reorganization in Escherichia coli complex I due to redox-driven proton translocation. Biopolymers 74:69-72
Abstract	The proton-pumping NADH:ubiquinone oxidoreductase (complex I) couples the transfer of electrons from NADH to ubiquinone with the translocation of protons across the membrane. Electron transfer is accomplished by flavin mononucleotide (FMN) and a series of iron-sulfur (Fe/S) clusters. A novel mechanism has been proposed wherein the electron transfer reaction induces conformational changes that subsequently lead to the translocation of protons. Redox-induced Fourier transform infrared difference spectra have been obtained, showing strong conformational changes in the amide I region. The amplitude of the signal is pH dependent, as expected for an energy coupling step in the enzymes reaction. Furthermore, pH-dependent protonation events and quinone binding were detected.
Links	PubMed Online version:10.1002/bip.20046
Keywords	Amides/chemistry; Benzoquinones/chemistry; Electrochemistry; Electrons; Escherichia coli/metabolism; Escherichia coli Proteins; Flavin Mononucleotide/chemistry; Hydrogen-Ion Concentration; NAD/chemistry; Oxidation-Reduction; Protein Conformation; Protein Transport; Protons; Quinones/chemistry; Spectroscopy, Fourier Transform Infrared/methods; Transcription Factors/chemistry
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