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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1489-1494
Number of pages6
Issue number3
Publication statusPublished - 2005 May

ASJC Scopus subject areas

  • Organic Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Polymers and Plastics
  • Materials Chemistry


Dive into the research topics of 'Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin'. Together they form a unique fingerprint.

Cite this