Involvement of a Glu71-Arg64 Couple in the Access Channel for NADH in Cytochrome P450nor

• SU Fei

  Institute of Applied Biochemistry, University of Tsukuba

• FUSHINOBU Shinya

  Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo

• TAKAYA Naoki

  Institute of Applied Biochemistry, University of Tsukuba

• SHOUN Hirofumi

  Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo

抄録

Putative access channel for NADH in the heme-distal pocket of cytochrome P450nor (P450nor) comprises many charged amino acid residues. Characterization of the E71A mutant protein of P450nor highlights the existence of a unique mechanism for binding NADH that depends on the salt bridge network between Glu71, Arg64 and Asp88.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 68 (5), 1156-1159, 2004

  公益社団法人 日本農芸化学会

キーワード

• cytochrome P450nor
• NADH binding
• nitric oxide reductase
• salt bridge network

詳細情報

• CRID: 1390001206473967360
• NII論文ID: 130000030748
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.68.1156
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 6957592
• PubMed: 15170127
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6957592
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.68.1156
• 本文言語コード: en
• データソース種別:
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  • NDL
  • Crossref
  • PubMed
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• 抄録ライセンスフラグ: 使用不可