論文

査読有り
2006年3月

Specific binding of CO to tetraheme cytochrome c(3)

BIOCHEMISTRY
  • Y Takayama
  • ,
  • Y Kobayashi
  • ,
  • N Yahata
  • ,
  • T Saitoh
  • ,
  • H Hori
  • ,
  • T Ikegami
  • ,
  • H Akutsu

45
10
開始ページ
3163
終了ページ
3169
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1021/bi051867i
出版者・発行元
AMER CHEMICAL SOC

Carbon monoxide (CO) has been identified as another bioactive molecule like NO. Binding of CO to a tetraheme cytochiome c(3) (cyt c(3)) was investigated using visible absorption spectroscopy, circular dichroism (CD), and NMR. CO was found to bind to the four hemes in different manners. CD spectra, however, indicated that only single-site CO binding can keep the protein intact. The K-d for the single-site binding was 8.0 mu M, which is a typical value for a CO sensor protein. Furthermore, NMR spectra of uniformly N-15-labeled and specifically [N-15]His-labeled proteins have provided evidence that CO specifically binds to the sixth coordination site of heme 2 via single-site binding. The CO-bound cyt c(3) could conduct redox reactions. In light of triheme cytochrome c(7), the CO-bound cyt c(3) may work as an electron transporter. It was reported for sulfate-reducing bacteria that CO can be used as an energy source and CO cycling is operating like H-2 cycling. Therefore, the CO-bound cyt c(3) may play a role in maintaining electron transport pathways on accumulation of toxic CO for its utilization.

Web of Science ® 被引用回数 : 11

リンク情報
DOI
https://doi.org/10.1021/bi051867i
CiNii Articles
http://ci.nii.ac.jp/naid/30010865899
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/16519511
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000236015100006&DestApp=WOS_CPL
ID情報
  • DOI : 10.1021/bi051867i
  • ISSN : 0006-2960
  • CiNii Articles ID : 30010865899
  • PubMed ID : 16519511
  • Web of Science ID : WOS:000236015100006

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