A ferredoxin Arg‐Glu pair important for efficient electron transfer between ferredoxin and ferredoxin‐NADP+ reductase

FEBS Letters

Hase, Toshiharu¹  Kimata-Ariga, Yoko¹  Fujita, Shinobu²  Teshima, Keizo²  Nishiyama, Daisuke³  Kusunoki, Masami³  Hirose, Syuuichi²  Kurisu, Genji³ 

[1] Division of Enzymology, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan;Faculty of Integrated Arts and Sciences, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima 739-8521, Japan;Research Center for Structural and Functional Proteomics, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan

关键词: Ferredoxin;    Ferredoxin-NADP+ reductase;    Electron transfer;    Photosynthesis;    Equisetum arvense;    DTT;    dithiothreitol;    Fd;    ferredoxin;    FNR;    ferredoxin-NADP+ oxidoreductase;    MALDI-TOF;    matrix-assisted laser desorption/ionization time of flight;   

DOI  :  10.1016/S0014-5793(03)00559-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In order to elucidate the importance of a ferredoxin (Fd) Arg-Glu pair involved in dynamic exchange from intra- to intermolecular salt bridges upon complex formation with ferredoxin-NADP⁺ oxidoreductase (FNR), Equisetum arvense FdI and FdII were investigated as normal and the pair-lacking Fd, respectively. The FdI mutant lacking this pair was unstable and rapidly lost the [2Fe–2S] cluster. The catalytic constant (k _cat) of the electron transfer for FdI is 5.5 times that for FdII and the introduction of this pair into FdII resulted in the increase of k _cat to a level comparable to that for FdI, demonstrating directly that the Arg-Glu pair is important for efficient electron transfer between Fd and FNR.

【 授权许可】

Unknown