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Galactose oxidase model studies

Ligands to Metal in Galactose Oxidase ESR and Model Studies... [Pg.267]

Zurita, D., Scheer, C., Pierre, J.-L., and Saint-Aman, E., 1996, Solution Studies of Copper(II) Complexes as Models for the Active Site of Galactose Oxidase, J. Chem. Soc., Dalton Trans. 4331n4336. [Pg.231]

Jazdzewski BA, Tolma WB (2000) Understanding the copper-phenoxyl radical array in galactose oxidase contributions from synthetic modeling studies. Coord Chem Rev 200-202 633-685... [Pg.34]

Two phenoxyl radical complexes [Cu (2 )N03] and [Zn (2 )N03] oxidize benzyl alcohol to benzaldehyde and have been studied as models for the enzyme galactose oxidase (GO). GO contains a dipeptide unit (3) in which a tyrosine residue is covalently bound to an adjacent cysteine residue and which is similar to (2), the tyrosyl radical in (3) also being bound to the Cu centre (see Figure 1). Second-order kinetics were observed with respect to [Zn°(2 )N03]+ and there was no evidence of redox reaction at the zinc site, suggesting that a dimeric form of the complex is active however, the reaction of [Cu H2 )N03]+ with benzyl alcohol is first order in the metal complex and [Cu (2H)]+ is identified as a product, suggesting a formal 2e /2H+ mechanism in which the monomeric form coordinates the alcohol in the manner believed to operate for G0. 2... [Pg.209]


See other pages where Galactose oxidase model studies is mentioned: [Pg.89]    [Pg.273]    [Pg.614]    [Pg.825]    [Pg.525]    [Pg.294]    [Pg.265]    [Pg.77]    [Pg.5792]    [Pg.2397]    [Pg.146]    [Pg.603]    [Pg.793]    [Pg.506]    [Pg.5791]    [Pg.5805]    [Pg.13]    [Pg.15]    [Pg.201]    [Pg.398]    [Pg.186]    [Pg.365]    [Pg.15]   


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Galactose oxidase

Model studies

Modeling studies

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