COMPARISON OF THE BINDING-SITES OF PLANT FERREDOXIN FOR 2 FERREDOXIN-DEPENDENT ENZYMES

被引：30

作者：

DEPASCALIS, AR

SCHURMANN, P

BOSSHARD, HR

机构：

[1] UNIV ZURICH,INST BIOCHEM,CH-8057 ZURICH,SWITZERLAND

[2] UNIV NEUCHATEL,BIOCHIM LAB,CH-2000 NEUCHATEL,SWITZERLAND

来源：

FEBS LETTERS | 1994年 / 337卷 / 03期

关键词：

CARBOXYL GROUP; CHEMICAL MODIFICATION; ELECTROSTATIC INTERACTION; FERREDOXIN (SPINACH); FERREDOXIN-THIOREDOXIN REDUCTASE (SPINACH); FERREDOXIN-NADP(+) REDUCTASE (SPINACH);

D O I：

10.1016/0014-5793(94)80194-0

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：

Differential chemical modification of acidic residues was used to map the binding site of plant ferredoxin (Fd) for the chloroplast enzyme ferredoxin:thioredoxin reductase (FTR). Binding of FTR to Fd inhibits chemical modification of Fd residues D34, D65, E92, E93, E94 and C-terminal A97. The binding site demarcated by these residues differs from that for ferredoxin:NADP(+) reductase (FNR). The FTR site includes C-terminal residues but not helix 24-31, which is part of the FNR site. Both sites enclose the [2Fe-2S] cluster.

引用

页码：217 / 220

页数：4

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