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Insights into the ubiquinol/dioxygen binding and proton relay pathways of the alternative oxidase.
Shiba, Tomoo; Inaoka, Daniel Ken; Takahashi, Gen; Tsuge, Chiaki; Kido, Yasutoshi; Young, Luke; Ueda, Satoshi; Balogun, Emmanuel Oluwadare; Nara, Takeshi; Honma, Teruki; Tanaka, Akiko; Inoue, Masayuki; Saimoto, Hiroyuki; Harada, Shigeharu; Moore, Anthony L; Kita, Kiyoshi.
Affiliation
  • Shiba T; Department of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Sakyo-ku, Matsugasaki, Kyoto 606-8585, Japan. Electronic address: tshiba@kit.ac.jp.
  • Inaoka DK; School of Tropical Medicine and Global Health, Nagasaki University, Sakamoto 1-12-4, Nagasaki 852-8523, Japan; Department of Host-Defense Biochemistry, Institute of Tropical Medicine (NEKKEN), Nagasaki University, Sakamoto 1-12-4, Nagasaki 852-8523, Japan; Department of Biomedical Chemistry, Graduat
  • Takahashi G; Department of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Sakyo-ku, Matsugasaki, Kyoto 606-8585, Japan.
  • Tsuge C; Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Hongo 7-3-1, Tokyo 113-0033, Japan.
  • Kido Y; School of Tropical Medicine and Global Health, Nagasaki University, Sakamoto 1-12-4, Nagasaki 852-8523, Japan; Department of Parasitology, Graduate School of Medicine, Osaka City University, Abeno-ku, Asahimachi 1-4-3, Osaka 545-8585, Japan.
  • Young L; Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, UK.
  • Ueda S; Department of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Sakyo-ku, Matsugasaki, Kyoto 606-8585, Japan.
  • Balogun EO; Department of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Sakyo-ku, Matsugasaki, Kyoto 606-8585, Japan; Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Hongo 7-3-1, Tokyo 113-0033, Japan; Department o
  • Nara T; Department of Molecular and Cellular Parasitology, Juntendo University School of Medicine, Bunkyo-ku, Hongo 2-1-1, Tokyo, 113-8421, Japan.
  • Honma T; Systems and Structural Biology Center, RIKEN, Tsurumi, Suehiro 1-7-22, Yokohama, Kanagawa 230-0045, Japan.
  • Tanaka A; Systems and Structural Biology Center, RIKEN, Tsurumi, Suehiro 1-7-22, Yokohama, Kanagawa 230-0045, Japan.
  • Inoue M; Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Hongo 7-3-1, Tokyo 113-0033, Japan.
  • Saimoto H; Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Koyamacho-Minami 4, Tottori 680-8552, Japan.
  • Harada S; Department of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Sakyo-ku, Matsugasaki, Kyoto 606-8585, Japan.
  • Moore AL; Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, UK.
  • Kita K; School of Tropical Medicine and Global Health, Nagasaki University, Sakamoto 1-12-4, Nagasaki 852-8523, Japan; Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Hongo 7-3-1, Tokyo 113-0033, Japan; Department of Host-Defense Biochemistry, Institute o
Biochim Biophys Acta Bioenerg ; 1860(5): 375-382, 2019 05 01.
Article in En | MEDLINE | ID: mdl-30910528
ABSTRACT
The alternative oxidase (AOX) is a monotopic diiron carboxylate protein which catalyzes the four-electron reduction of dioxygen to water by ubiquinol. Although we have recently determined the crystal structure of Trypanosoma brucei AOX (TAO) in the presence and absence of ascofuranone (AF) derivatives (which are potent mixed type inhibitors) the mechanism by which ubiquinol and dioxygen binds to TAO remain inconclusive. In this article, ferulenol was identified as the first competitive inhibitor of AOX which has been used to probe the binding of ubiquinol. Surface plasmon resonance reveals that AF is a quasi-irreversible inhibitor of TAO whilst ferulenol binding is completely reversible. The structure of the TAO-ferulenol complex, determined at 2.7 Å, provided insights into ubiquinol binding and has also identified a potential dioxygen molecule bound in a side-on conformation to the diiron center for the first time.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oxidoreductases / Oxygen / Plant Proteins / Trypanosoma brucei brucei / Protozoan Proteins / Ubiquinone / Mitochondrial Proteins Language: En Journal: Biochim Biophys Acta Bioenerg Year: 2019 Document type: Article
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oxidoreductases / Oxygen / Plant Proteins / Trypanosoma brucei brucei / Protozoan Proteins / Ubiquinone / Mitochondrial Proteins Language: En Journal: Biochim Biophys Acta Bioenerg Year: 2019 Document type: Article