ELECTRON-SPIN ECHO STUDIES OF THE COPPER-BINDING SITE IN PHENYLALANINE-HYDROXYLASE FROM CHROMOBACTERIUM-VIOLACEUM
ELECTRON-SPIN ECHO STUDIES OF THE COPPER-BINDING SITE IN PHENYLALANINE-HYDROXYLASE FROM CHROMOBACTERIUM-VIOLACEUM
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DOI:
10.1021/ja00212a012
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发表时间:
1988-02-17
影响因子:
15
通讯作者:
PEISACH, J
中科院分区:
文献类型:
--
作者:
MCCRACKEN, J;PEMBER, S;PEISACH, J
The active-site structure of the Cu(II)-containing phenylalanine hydroxylase from Chromobacterium violaceum was studied by electron spin-echo spectroscopy. Fourier transformation of the stimulated electron spin-echo envelope for the copper protein revealed frequency components characteristics of copper-histidyl imidazole coordination. The observed nuclear quadrupole frequencies at 0.55, 1.0, and 1.55 MHz are slightly different from those observed for model Cu(II)-imidazole complexes, 0.68, 0.72, and 1.40 MHz, but can be observed in Cu(II) complexes with 2-methylimidazole. A method of analysis by spectral simulation is presented for the quantitation of the number of equatorial imidazoles coordinated to Cu (II). In phenylalanine hydroxylase, two are bound.