論文

査読有り
2006年4月

NMR study of the electron transfer complex of plant ferredoxin and sulfite reductase - Mapping the interaction sites of ferredoxin

JOURNAL OF BIOLOGICAL CHEMISTRY
  • T Saitoh
  • ,
  • T Ikegami
  • ,
  • M Nakayama
  • ,
  • K Teshima
  • ,
  • H Akutsu
  • ,
  • T Hase

281
15
開始ページ
10482
終了ページ
10488
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1074/jbc.M510530200
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Plant ferredoxin serves as the physiological electron donor for sulfite reductase, which catalyzes the reduction of sulfite to sulfide. Ferredoxin and sulfite reductase form an electrostatically stabilized 1:1 complex for the intermolecular electron transfer. The protein-protein interaction between these proteins from maize leaves was analyzed by nuclear magnetic resonance spectroscopy. Chemical shift perturbation and cross-saturation experiments successfully mapped the location of two major interaction sites of ferredoxin: region 1 including Glu-29, Glu-30, and Asp-34 and region 2 including Glu-92, Glu-93, and Glu-94. The importance of these two acidic patches for interaction with sulfite reductase was confirmed by site-specific mutation of acidic ferredoxin residues in regions 1 and 2, separately and in combination, by which the ability of mutant ferredoxins to transfer electrons and bind to sulfite reductase was additively lowered. Taken together, this study gives a clear illustration of the molecular interaction between ferredoxin and sulfite reductase. We also present data showing that this interaction surface of ferredoxin significantly differs from that when ferredoxin-NADP(+) reductase is the interaction partner.

Web of Science ® 被引用回数 : 38

リンク情報
DOI
https://doi.org/10.1074/jbc.M510530200
CiNii Articles
http://ci.nii.ac.jp/naid/30016364003
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/16469743
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000236594300077&DestApp=WOS_CPL
ID情報
  • DOI : 10.1074/jbc.M510530200
  • ISSN : 0021-9258
  • CiNii Articles ID : 30016364003
  • PubMed ID : 16469743
  • Web of Science ID : WOS:000236594300077

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