Cytochrome oxidases concerted electron transfer

Laccase, 6,699 copper, 6,654 cytochrome oxidases concerted electron transfer, 6,683 fungal... 

Fig. 3.3. Tentative mechanism of reduction of dioxygen. The scheme shows some of the more significant reaction steps at the haem iron-Cug centre of cytochrome oxidase. The reaction may be initiated by delivery of dioxygen to the reduced enzyme (in anaerobiosis top of figure). An initially formed oxy intermediate is normally extremely short-lived, but can be stabilised and identified in artificial conditions (see Refs. 92, 99,129, 134). Concerted transfer of two electrons from Fe and Cu to bound dioxygen yields a peroxy intermediate. This, or its electronic analogue, is stabilised in the absence of electron donors (ferrocytochrome a and/or reduced Cu ), and has been termed Compound C [129,130,132). It may also be observed at room temperature, and is then probably generated from the oxidised state by partial oxidation of water in the active site, in an energy-linked reversed electron transfer reaction [29] (see also Refs. 92, 99). Also the ferryl intermediate [92,99,100] has been tentatively observed in such conditions [29]. In aerobic steady states the reaction is thought to involve the cycle of intermediates in the centre of the figure (dark frames). The irreversible step is probably the conversion of g = 6 (see Refs. 98, 133) to peroxy .

The two metal ions also function in concert in proteins such as cytochrome oxidase, which catalyzes the transfer of four electrons to dioxygen to form water during respiration. Whether any types of biological reactions are unique to copper proteins is not clear. However, use of stored iron is reduced by copper deficiency, which suggests that iron metabolism may depend on copper proteins. 

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