OVEREXPRESSION OF DESULFOVIBRIO-VULGARIS HILDENBOROUGH CYTOCHROME-C(553) IN DESULFOVIBRIO-DESULFURICANS G200 - EVIDENCE OF CONFORMATIONAL HETEROGENEITY IN THE OXIDIZED PROTEIN BY NMR

被引:23
作者
BLANCHARD, L
MARION, D
POLLOCK, B
VOORDOUW, G
WALL, J
BRUSCHI, M
GUERLESQUIN, F
机构
[1] LAB CHIM BACTERIENNE,CNRS,CHEMIN JOSEPH AIGUIER,BP71,F-13277 MARSEILLE,FRANCE
[2] CEA,INST BIOL STRUCT,CNRS,GRENOBLE,FRANCE
[3] UNIV CALGARY,DEPT BIOL SCI,DIV BIOCHEM,CALGARY T2N 1N4,ALBERTA,CANADA
[4] UNIV MISSOURI,DEPT BIOCHEM,COLUMBIA,MO 65201
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1993年 / 218卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1993.tb18377.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Plasmid pRC41, containing the cyf gene encoding cytochrome c553 from Desulfovibrio vulgaris Hildenborough, was transferred by conjugation from Escherichia coli to Desulfovibrio desulfuricans G200. The structural properties of the purified protein were studied by one-dimensional and two-dimensional NMR. A heterogeneity in the folding of the cytochrome isolated from D. vulgaris Hildenborough and from D. desulfuricans G200 was observed for the oxidized form. Temperature, pH and salt-dependence studies indicated that the heterogeneity does not result from an intermediate in the protein unfolding process, but derives from two conformations which are not in dynamic equilibrium.
引用
收藏
页码:293 / 301
页数:9
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