caa a22 4500 475845935 CHVBK 20180406123914.0 cr unu---uuuuu 170329e20000901xx s 000 0 eng 10.1007/PL00000631 doi (NATIONALLICENCE)springer-10.1007/PL00000631 The ratio between the fast and slow forms of bovine cytochrome c oxidase is changed by cholate or nucleotides bound to the cholate-binding site close to the cytochrome a3/CuB binuclear centre [Elektronische Daten] [K. Shoji, A. Giuffrè, E. D'Itri, K. Hagiwara, T. Yamanaka, M. Brunori*, P. Sarti] Abstract.: We determined the fraction of ‘slow' and ‘fast' conformations of bovine cytochrome c oxidase, following the kinetics of cyanide binding to the oxidized enzyme. We investigated whether treatment of heart mitochondrial particles with different commercially available types of cholate (standard and ultra-pure) can affect the fraction of cytochrome c oxidase in the two states. Compared to standard cholate, the use of ultra-pure cholate for solubilization of heart mitochondrial particles significantly increased the fraction of the fast enzyme. Complete homogeneity (∼100% fast) was observed when cytochrome c oxidase was solubilized with ultra-pure cholate from heart mitochondrial particles pre-equilibrated with AMP; equilibration with ADP yielded a much smaller fraction of fast enzyme (∼35%). These observations are discussed on the basis of the structural relationships between the known cholate-binding site and the binuclear cytochrome a3-CuB site: variation in the occupancy of this binding site with cholate or nucleotides may modify reactivity of the oxidized binuclear centre towards cyanide. Birkhäuser Verlag Basel,, 2000 Key words. Mitochondrial particles nationallicence cytochrome oxidase nationallicence fast and slow conformation nationallicence cyanide binding nationallicence nucleotides nationallicence cholate nationallicence structure nationallicence Shoji K. Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Kanda-Surugadai 1-5, Chiyoda-ku, Tokyo 101-8308 (Japan), JP aut Giuffrè A. Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome "La Sapienza”, Piazzale Aldo Moro 5, I-00185 (Rome, Italy), Fax +39 06 4440062, e-mail: maurizio.brunori@uniroma1.it, IT aut D'Itri E. Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome "La Sapienza”, Piazzale Aldo Moro 5, I-00185 (Rome, Italy), Fax +39 06 4440062, e-mail: maurizio.brunori@uniroma1.it, IT aut Hagiwara K. Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Kanda-Surugadai 1-5, Chiyoda-ku, Tokyo 101-8308 (Japan), JP aut Yamanaka T. Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Kanda-Surugadai 1-5, Chiyoda-ku, Tokyo 101-8308 (Japan), JP aut Brunori* M. Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome "La Sapienza”, Piazzale Aldo Moro 5, I-00185 (Rome, Italy), Fax +39 06 4440062, e-mail: maurizio.brunori@uniroma1.it, IT aut Sarti P. Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome "La Sapienza”, Piazzale Aldo Moro 5, I-00185 (Rome, Italy), Fax +39 06 4440062, e-mail: maurizio.brunori@uniroma1.it, IT aut https://doi.org/10.1007/PL00000631 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/PL00000631 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Shoji K. Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Kanda-Surugadai 1-5, Chiyoda-ku, Tokyo 101-8308 (Japan), JP aut NATIONALLICENCE 700 1- Giuffrè A. Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome "La Sapienza”, Piazzale Aldo Moro 5, I-00185 (Rome, Italy), Fax +39 06 4440062, e-mail: maurizio.brunori@uniroma1.it, IT aut NATIONALLICENCE 700 1- D'Itri E. Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome "La Sapienza”, Piazzale Aldo Moro 5, I-00185 (Rome, Italy), Fax +39 06 4440062, e-mail: maurizio.brunori@uniroma1.it, IT aut NATIONALLICENCE 700 1- Hagiwara K. Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Kanda-Surugadai 1-5, Chiyoda-ku, Tokyo 101-8308 (Japan), JP aut NATIONALLICENCE 700 1- Yamanaka T. Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Kanda-Surugadai 1-5, Chiyoda-ku, Tokyo 101-8308 (Japan), JP aut NATIONALLICENCE 700 1- Brunori* M. Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome "La Sapienza”, Piazzale Aldo Moro 5, I-00185 (Rome, Italy), Fax +39 06 4440062, e-mail: maurizio.brunori@uniroma1.it, IT aut NATIONALLICENCE 700 1- Sarti P. Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome "La Sapienza”, Piazzale Aldo Moro 5, I-00185 (Rome, Italy), Fax +39 06 4440062, e-mail: maurizio.brunori@uniroma1.it, IT aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer