Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin

Teruyuki Komatsu, Seiji Ishihara, Eishun Tsuchida, Hiroyuki Nishide*, Chihiro Morokuma, Satoshi Nakamura

*この研究の対応する著者

研究成果: Article査読

12 被引用数 (Scopus)

抄録

Synthetic iron(II) porphyrin (FeP) is equivalently incorporated into recombinant Thermotoga maritima xylanase B (TMX; family F/10 of glycoside hydrolase), producing a heat-resistant artificial hemoprotein (TMX-FeP) that can bind and release oxygen (O2) in aqueous medium (pH 7.3, 25 °C) in the same manner as hemoglobin and myoglobin. The oxygenated species was sufficiently stable; the half-lifetime against the ferric state (τ1/2) was 5 h. This O2-carrying hemoprotein showed a high degree of thermal stability over a wide range of temperatures up to 90 °C (τ1/2 = 5 min at 90 °C and 9 min at 75 °C). Dictyoglomus thermophilum xylanase B (DTX; family G/11) also incorporates FeP, and DTX-FeP showed identical O2-binding parameters and thermostability. TMX-FeP is capable of catalyzing the β-1,4-D-xylan hydrolysis reaction. Its larger Km value compared to that of TMX itself suggested competitive FeP binding to the active site of the host enzyme.

本文言語English
ページ(範囲)1489-1494
ページ数6
ジャーナルBiomacromolecules
6
3
DOI
出版ステータスPublished - 2005 5月

ASJC Scopus subject areas

  • 有機化学
  • 生化学、遺伝学、分子生物学(全般)
  • ポリマーおよびプラスチック
  • 材料化学

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