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Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system

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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 H2O/D2O 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.

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Abbreviations

FMN:

Flavin mononucleotide

PHBH:

para-hydroxybenzoate hydroxylase

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Authors and Affiliations

  1. Department of Life Science, Graduate School of Life Science, University of Hyogo, Koto 3-2-1, Kamigori-cho, Ako-gun, Hyogo, 678-1297, Japan

    Hidehisa Sugiyama, Ryohei Nakatsubo, Satoru Yamaguchi, Takashi Ogura, Kyoko Shinzawa-Itoh & Shinya Yoshikawa

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  1. Hidehisa Sugiyama
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  2. Ryohei Nakatsubo
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  3. Satoru Yamaguchi
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  4. Takashi Ogura
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  5. Kyoko Shinzawa-Itoh
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  6. Shinya Yoshikawa
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Corresponding author

Correspondence to Takashi Ogura.

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Sugiyama, H., Nakatsubo, R., Yamaguchi, S. et al. Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone oxidoreductase, the largest membrane protein in the mitochondrial respiratory system. J Bioenerg Biomembr 39, 145–148 (2007). https://doi.org/10.1007/s10863-007-9072-3

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  • DOI: https://doi.org/10.1007/s10863-007-9072-3

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