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Rate constants azurin systems

Direct evidence for long range electron-transfer in biological systems was first observed by Gray et al.50,51) and Isied et al.481 using [Ru(NH3)5]3+ substituted metallo protein. Histidine-83 of blue copper (azurin) was labeled with Ru(III)(NH3)5 50). Flash photolysis reduction of the His-83 bound Ru(III) followed by electron-transfer from the Ru(II) to Cu2+ was observed with a rate constant of 1.9 s 1. The result shows that intramolecular long distance (approx. 1 nm) electron-transfer from the Ru(II) to the Cu2 + of the azurin takes place rapidly. [Pg.117]


See other pages where Rate constants azurin systems is mentioned: [Pg.178]    [Pg.297]    [Pg.297]    [Pg.290]    [Pg.129]    [Pg.18]    [Pg.23]    [Pg.570]    [Pg.71]    [Pg.72]    [Pg.572]    [Pg.201]    [Pg.5322]    [Pg.5323]    [Pg.5323]    [Pg.18]    [Pg.19]    [Pg.19]    [Pg.7]    [Pg.237]    [Pg.58]    [Pg.1852]   
See also in sourсe #XX -- [ Pg.22 , Pg.23 ]




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