A consensus structure for the active site of terminal oxidases has been recently proposed by Hosler et al. [(1993) J. Bioenerg. Biomem. 25, 121-135]. We exploit the novel structural information to propose a hypothesis for the large difference in the rate of internal electron transfer found when experiments are started either with the reduced or with the oxidized enzyme. This rationale also allows us to discuss the oxidation state of the prevailing oxygen reacting species with reference to the concentration of the two substrates (oxygen and cytochrome c) and to the structural state of the oxidase
Electron transfer and ligand binding in terminal oxidases. Impact of recent structural information / Brunori, Maurizio; Antonini, G; Giuffre', Alessandro; Malatesta, Francesco; Nicoletti, F; Sarti, Paolo; Wilson, Mt. - In: FEBS LETTERS. - ISSN 0014-5793. - 350:(1994), pp. 164-168. [10.1016/0014-5793(94)00779-9]
Electron transfer and ligand binding in terminal oxidases. Impact of recent structural information
BRUNORI, Maurizio;GIUFFRE', ALESSANDRO;MALATESTA, FRANCESCO;SARTI, Paolo;
1994
Abstract
A consensus structure for the active site of terminal oxidases has been recently proposed by Hosler et al. [(1993) J. Bioenerg. Biomem. 25, 121-135]. We exploit the novel structural information to propose a hypothesis for the large difference in the rate of internal electron transfer found when experiments are started either with the reduced or with the oxidized enzyme. This rationale also allows us to discuss the oxidation state of the prevailing oxygen reacting species with reference to the concentration of the two substrates (oxygen and cytochrome c) and to the structural state of the oxidaseI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
