Reaction of Nitric Oxide with the Turnover Intermediates of Cytochrome c Oxidase: Reaction Pathway and Functional Effects

Autor: Giuffrè A, Barone MC, Mastronicola D, D'Itri E, Sarti P, Brunori, M

Publikováno v: Biochemistry (Easton) 39 (2000): 15446–15453. doi:10.1021/bi000447k
info:cnr-pdr/source/autori:Giuffrè A, Barone MC, Mastronicola D, D'Itri E, Sarti P, Brunori, M/titolo:Reaction of nitric oxide with the turnover intermediates of cytochrome c oxidase: Reaction pathway and functional effects/doi:10.1021%2Fbi000447k/rivista:Biochemistry (Easton)/anno:2000/pagina_da:15446/pagina_a:15453/intervallo_pagine:15446–15453/volume:39

The reactions of nitric oxide (NO) with the turnover intermediates of cytochrome c oxidase were investigated by combining amperometric and spectroscopic techniques. We show that the complex of nitrite with the oxidized enzyme (O) is obtained by react

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eab15339dd2a458715b2140f719e8c13
https://doi.org/10.1021/bi000447k

L-carnitine (CAR) affects locomotor activity (LMA) in homozygous transgenic mice that express the Q340H mutated human TRbeta-1 protein, a mutation associated with both thyroid hormone resistance (RTH) and attention deficit/hyperactivity disorder (ADHD)

Autor: Benvenga, Salvatore, Itri, E, Pappalardo, maria angela, DE TOLLA, L, S. F., Yu, Hauser, P, Testa, G, Trimarchi, F, Amato, A.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3978::a174ae343d14e05a4d47211013d54df1
http://hdl.handle.net/11570/1677735

Transgenic homozygous mice harboring a mutated TRbeta1 CDNA maintain, lose or acquire sexual dimorphism in locomotor activities (LMA)

Autor: Benvenga, Salvatore, Itri, E, Pappalardo, maria angela, DE TOLLA, L, S. F., Yu, Hauser, P, Trimarchi, F, Amato, A.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3978::891bf70bf7f420fe79a2b65e33e4ff38
http://hdl.handle.net/11570/1677714

Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants

Autor: Forte E, Scandurra FM, Richter OM, D'Itri E, Sarti P, Brunori M, Ludwig B, Giuffrè A.

Publikováno v: Biochemistry (Easton) 43 (2004): 2957–2963.
info:cnr-pdr/source/autori:Forte E; Scandurra FM; Richter OM; D'Itri E; Sarti P; Brunori M; Ludwig B; Giuffrè A./titolo:Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants./doi:/rivista:Biochemistry (Easton)/anno:2004/pagina_da:2957/pagina_a:2963/intervallo_pagine:2957–2963/volume:43

The kinetics and stoichiometry of the redox-linked protonation of the soluble Paracoccus denitrificans cytochrome c oxidase were investigated at pH ) 7.2-7.5 by multiwavelength stopped-flow spectroscopy, using the pH indicator phenol red. We compared

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::f8ee3e174da173f82ef4b5a8e831b2e7
http://www.cnr.it/prodotto/i/11694

Proton uptake upon anaerobic reduction of the paracoccus denitrificans cytochrome c oxidase

Autor: Giuffre', Alessandro, Forte, Elena, Scandurra, Fm, Richter, Oh, D'Itri, E, Sarti, Paolo, Ludwig, B., Brunori, M.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3686::e9346198bf2778098dd3083be743ea81
http://hdl.handle.net/11573/470431