COORDINATION OF AMINO-ACIDS BY THE FE-3+ PORPHYRIN MICROPEROXIDASE-8 - POSSIBLE ROLE FOR THE INVARIANT PHE IN THE PEROXIDASE ENZYMES

被引:16
作者
BYFIELD, MP [1 ]
PRATT, JM [1 ]
机构
[1] UNIV SURREY, DEPT CHEM, GUILDFORD GU2 5XH, SURREY, ENGLAND
关键词
D O I
10.1039/c39920000214
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Equilibrium constants have been determined for the substitution of coordinated H2O in the Fe3+ MP-8 by various amino acids in 20% aqueous MeOH at 25-degrees-C; the presence of an aromatic side chain significantly increases log K from, e.g. Gly 3.5 to Phe 4.8 and Trp 5.6 and causes a shift in the wavelength of the Soret band from 403 to 406 nm, which is ascribed to donor-acceptor interaction between the porphyrin and aromatic/heterocyclic rings and suggests a role for the invariant distal Phe in the peroxidases.
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页码:214 / 215
页数:2
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