Comparison of the binding sites of plant ferredoxin for two ferredoxin‐dependent enzymes

FEBS Letters

Schürmann, P.²  Bosshard, H.R.¹  De Pascalis, A.R.¹ 

[1] Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland;Laboratoire de Biochimie, Université de Neuchâtel, Ch. de Chantemerle 18, CH-2000 Neuchâtel, Switzerland

关键词: Carboxyl group;    Chemical modification;    Electrostatic interaction;    Ferredoxin (spinach);    Ferredoxin:thioredoxin reductase (spinach);    FerredoxmNADP+ reductase (spinach);    EDC;    1-ethyl-3-(3-dimethylaminopropyl)carbodiinude;    Fd;    ferredoxin;    FNR;    ferredoxin:NADP+ reductase (EC 1.18.1.2);    FTR;    ferredoxin:thioredoxin reductase;   

DOI  :  10.1016/0014-5793(94)80194-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown