title: Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system.
abstract: The resonance Raman spectra of FMN of the bovine heart NADH: ubiquinone oxidoreductase with the molecular mass of approximately one million dalton were determined by using highly improved enzyme preparation and resonance Raman apparatus. The band positions and the H(2)O/D(2)O exchange effect suggest that the N(3)-H group in the ring III of the isoalloxazine moiety is buried inside the protein to increase the vibrational coupling to the C(2)-N(3)-C(4) stretching mode and that the ring I is exposed to the aqueous phase.
authors: Department of Life Science, Graduate School of Life Science, University of Hyogo, Koto 3-2-1, Ako-gun, Hyogo 678-1297, Japan.
authors: Hidehisa
authors: H
authors: Sugiyama
authors: Ryohei
authors: R
authors: Nakatsubo
authors: Satoru
authors: S
authors: Yamaguchi
authors: Takashi
authors: T
authors: Ogura
authors: Kyoko
authors: K
authors: Shinzawa-Itoh
authors: Shinya
authors: S
authors: Yoshikawa
mesh_terms: D000818:Animals; D002417:Cattle; D042967:Electron Transport Complex I / Q000737:chemistry / Q000378:metabolism*; D005486:Flavin Mononucleotide / Q000737:chemistry / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000201:enzymology*; D024101:Mitochondrial Proteins / Q000737:chemistry / Q000378:metabolism*; D013059:Spectrum Analysis, Raman
chemical_list: D024101:Mitochondrial Proteins; D005486:Flavin Mononucleotide; D042967:Electron Transport Complex I