論文

査読有り
2012年5月

A new structural insight into differential interaction of cyanobacterial and plant ferredoxins with nitrite reductase as revealed by NMR and X-ray crystallographic studies

JOURNAL OF BIOCHEMISTRY
  • Yukiko Sakakibara
  • ,
  • Hitoshi Kimura
  • ,
  • Akira Iwamura
  • ,
  • Takashi Saitoh
  • ,
  • Takahisa Ikegami
  • ,
  • Genji Kurisu
  • ,
  • Toshiharu Hase

151
5
開始ページ
483
終了ページ
492
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1093/jb/mvs028
出版者・発行元
OXFORD UNIV PRESS

Ferredoxin (Fd), which plays a pivotal role in photosynthesis as an electron carrier, forms a transient complex with various Fd-dependent enzymes, such as nitrite reductase (NiR), to achieve efficient intermolecular electron transfer. We studied the protein-protein interaction of Fd and NiR by NMR spectroscopy and determined three acidic regions of Fd to be major sites for the interaction with NiR, indicating that the complex is stabilized through electrostatic interaction. During this study, we found Fds from higher plant and cyanobacterium, in spite of their high structural similarities including the above acidic regions, differ remarkably in the interaction with cyanobacterial NiR. In activity assay of NiR, K-m value for maize Fd (74.6 mu M) was 9.6 times larger than that for Leptolyngbya boryana Fd (7.8 mu M). The two Fds also showed a similar difference in binding assay to NiR-immobilized resin. Comparative site-specific mutagenesis of two Fds revealed that their discriminative ability for the interaction with NiR is attributed mainly to non-charged residues in the peripheral region of [2Fe-2S] cluster. These non-charged residues are conserved separately between Fds of plant and cyanobacterial origins. Our data highlight that intermolecular force(s) other than electrostatic attraction is(are) also crucial for the molecular interaction between Fd and partner enzyme.

Web of Science ® 被引用回数 : 24

リンク情報
DOI
https://doi.org/10.1093/jb/mvs028
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/22427434
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000303332400005&DestApp=WOS_CPL

エクスポート
BibTeX RIS