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Biogenesis of Cytochrome Oxidase

Biogenesis of Cytochrome Oxidase and Cytochrome b in Neurospora crassa... [Pg.125]

The simple coordination chemistry characteristic of the majority of protein-metal interactions is replaced in certain cases by irreversible covalent modifications of the protein mediated by the metal ion. These modifications are essential for the function and are templated by the structure of the protein, as no other proteins are required for the reaction to occur. These self-processing reactions result in the biogenesis of redox cofactors in some enzymes (amine oxidases, galactose oxidase, cytochrome c oxidase) and activation of hydrolytic sites in others (nitrile hydratase). The active sites of all of these enzymes are bifunctional, directing not only the catalytic turnover reaction of the mature enzyme but the modification steps required for maturation. [Pg.5500]


See other pages where Biogenesis of Cytochrome Oxidase is mentioned: [Pg.125]    [Pg.127]    [Pg.129]    [Pg.131]    [Pg.132]    [Pg.135]    [Pg.137]    [Pg.139]    [Pg.141]    [Pg.143]    [Pg.145]    [Pg.147]    [Pg.149]    [Pg.150]    [Pg.151]    [Pg.154]    [Pg.125]    [Pg.127]    [Pg.129]    [Pg.131]    [Pg.132]    [Pg.135]    [Pg.137]    [Pg.139]    [Pg.141]    [Pg.143]    [Pg.145]    [Pg.147]    [Pg.149]    [Pg.150]    [Pg.151]    [Pg.154]    [Pg.375]    [Pg.408]    [Pg.525]    [Pg.137]    [Pg.138]    [Pg.138]    [Pg.574]    [Pg.354]    [Pg.297]    [Pg.516]    [Pg.146]    [Pg.574]    [Pg.273]    [Pg.10]    [Pg.5]    [Pg.149]    [Pg.151]   


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Biogenesis

Biogenesis of Cytochrome

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