CINECA IRIS Institutional Research Information System
IRIS è la soluzione IT che facilita la raccolta e la gestione dei dati relativi alle attività e ai prodotti della ricerca. Fornisce a ricercatori, amministratori e valutatori gli strumenti per monitorare i risultati della ricerca, aumentarne la visibilità e allocare in modo efficace le risorse disponibili.
EnglishIn cytochrome c oxidase, oxido-reductions of heme a/CuA and heme a3/CuB are cooperatively linked to proton transfer at acid/base groups in the enzyme. H+/e− cooperative linkage at Fea3/CuB is envisaged to be involved in proton pump mechanisms confined to the binuclear center. Models have also been proposed which involve a role in proton pumping of cooperative H+/e− linkage at heme a (and CuA). Observations will be presented on: (i) proton consumption in the reduction of molecular oxygen to H2O in soluble bovine heart cytochrome c oxidase; (ii) proton release/uptake associated with anaerobic oxidation/reduction of heme a/CuA and heme a3/CuB in the soluble oxidase; (iii) H+ release in the external phase (i.e. H+ pumping) associated with the oxidative (R→O transition), reductive (O→R transition) and a full catalytic cycle (R→O→R transition) of membrane-reconstituted cytochrome c oxidase. A model is presented in which cooperative H+/e− linkage at heme a/CuA and heme a3/CuB with acid/base clusters, C1 and C2 respectively, and protonmotive steps of the reduction of O2 to water are involved in proton pumping.
Scheda prodotto non validato
Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo
| Titolo: | Concerted involvement of cooperative proton-electron linkage and water production in the proton pump of cytochrome c oxidase | |
| Autori: | ||
| Data di pubblicazione: | 2006 | |
| Rivista: | ||
| Abstract: | In cytochrome c oxidase, oxido-reductions of heme a/CuA and heme a3/CuB are cooperatively linked to proton transfer at acid/base groups in the enzyme. H+/e− cooperative linkage at Fea3/CuB is envisaged to be involved in proton pump mechanisms confined to the binuclear center. Models have also been proposed which involve a role in proton pumping of cooperative H+/e− linkage at heme a (and CuA). Observations will be presented on: (i) proton consumption in the reduction of molecular oxygen to H2O in soluble bovine heart cytochrome c oxidase; (ii) proton release/uptake associated with anaerobic oxidation/reduction of heme a/CuA and heme a3/CuB in the soluble oxidase; (iii) H+ release in the external phase (i.e. H+ pumping) associated with the oxidative (R→O transition), reductive (O→R transition) and a full catalytic cycle (R→O→R transition) of membrane-reconstituted cytochrome c oxidase. A model is presented in which cooperative H+/e− linkage at heme a/CuA and heme a3/CuB with acid/base clusters, C1 and C2 respectively, and protonmotive steps of the reduction of O2 to water are involved in proton pumping. | |
| Handle: | http://hdl.handle.net/11586/9572 | |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
File in questo prodotto:
Copyright © 2021