IDENTIFICATION OF 2FE-2S CYSTEINE LIGANDS IN PUTIDAREDOXIN

被引：27

作者：

GERBER, NC ^{[1
]}

HORIUCHI, T ^{[1
]}

KOGA, H ^{[1
]}

SLIGAR, SG ^{[1
]}

机构：

[1] KYUSHU UNIV,FAC PHARMACEUT SCI,HIGASHI KU,FUKUOKA 812,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 169卷 / 03期

关键词：

D O I：

10.1016/0006-291X(90)91995-5

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：

The iron-sulfur center of putidaredoxin is coordinated by four cysteine sulfhydrals. In order to determine which of the six cysteine residues in the protein coordinate the Fe-S center, we have individually mutated cysteine residues 73, 85 and 86 into serines. Of these mutant proteins, only C85S and C73S express holo-protein as evidenced by SDS-PAGE and EPR spectroscopy. This leads us to the conclusion that residues 39,45,48, and 86 are the cysteines that coordinate the iron-sulfur center in putidaredoxin. © 1990.

引用

页码：1016 / 1020

页数：5

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