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Azurin functional role

Blue copper proteins, 36 323, 377-378, see also Azurin Plastocyanin active site protonations, 36 396-398 charge, 36 398-401 classification, 36 378-379 comparison with rubredoxin, 36 404 coordinated amino acid spacing, 36 399 cucumber basic protein, 36 390 electron transfer routes, 36 403-404 electron transport, 36 378 EXAFS studies, 36 390-391 functional role, 36 382-383 occurrence, 36 379-382 properties, 36 380 pseudoazurin, 36 389-390 reduction potentials, 36 393-396 self-exchange rate constants, 36 401-403 UV-VIS spectra, 36 391-393 Blue species... [Pg.28]

Structure-function roles have been suggested for unique tryptophan residues in other copper proteins as well (44,45, 46). Moreover, the single tryptophan that is quenched by including the copper atom in azurin is apparently not in contact with the indole ring, as evidenced by metal replacement and phosphorescence results (45, 46). [Pg.280]

Summarizing the results of studies of intramolecular ET in azurins, it is important to stress that in all probability, the induced ET between the disulfide radical and the blue copper(II) center is not part of any physiological function, and the role of the disulfide is stmctural, solely. Still, azurin has turned out to be a very useful model system for examination of different parameters controlling LRET rates in proteins. The impact of specific stmctural changes introduced by single-site mutations has been studied in order to obtain a better understanding... [Pg.23]


See other pages where Azurin functional role is mentioned: [Pg.496]    [Pg.412]    [Pg.956]    [Pg.6220]    [Pg.71]    [Pg.373]    [Pg.955]    [Pg.6219]    [Pg.109]   
See also in sourсe #XX -- [ Pg.382 ]




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