Reduction of 2-carboxy-4'-dimethylaminoazobenzene by Bacillus diaphorase.

• Yatome Chizuko

  Department of Chemistry, Faculty of Engineering, Gifu University

• Ogawa Toshihiko

  Department of Chemistry, Faculty of Engineering, Gifu University

• Hayashi Hideki

  Department of Chemistry, Faculty of Engineering, Gifu University

Bibliographic Information

Other Title

• Reduction of 2-Carboxy-4′-dimethylaminoazobenzene by <i>Bacillus</i> Diaphorase

Abstract

2-Carboxy-4′-dimethylaminoazobenzene (CDMAB) was reductively cleaved into its two component primary arylamines by Bacillus diaphorase together with NADH (pH 6.1, 25 °C). The reductive cleavage was found to proceed stoichiometrically by a spectrofluorometric assay of fluorescent o-aminobenzoic acid and a fluorescent product formed between N,N-dimethyl-p-phenylenediamine and fluorescamine. Parallel lines were obtained in Lineweaver–Burk plots of initial rate vs. CDMAB concentration for the reduction. This experimentally observed kinetic behavior is consistent with a reaction scheme in favor of the Ping Pong mechanism in which CDMAB is reduced by a reduced form of diaphorase. From a kinetic formula, the apparent K_m(CDMAB), K_m(NADH), and V_max values are 2.14×10⁻⁵ mol dm⁻³, 7.35×10⁻⁵ mol dm⁻³, and 1.8×10⁻⁷ mol dm⁻³ min⁻¹ per mg of protein, respectively.

Journal

• Bulletin of the Chemical Society of Japan

  Bulletin of the Chemical Society of Japan 62 (4), 1123-1126, 1989

  The Chemical Society of Japan

Keywords

• General Chemistry

Details

• CRID: 1390282679106309248
• NII Article ID: 130001980568
• DOI: 10.1246/bcsj.62.1123
• ISSN: 13480634
• ISSN: 00092673
• Web Site: https://academic.oup.com/bcsj/article-pdf/62/4/1123/55727512/bcsj.62.1123.pdf
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed