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

doi:10.1021/bm049255l

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

Waseda Research Institute for Science and Engineering

Research output: Contribution to journal › Article › peer-review

14 Citations (Scopus)

Abstract

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 (τ_1/2) was 5 h. This O₂-carrying hemoprotein showed a high degree of thermal stability over a wide range of temperatures up to 90 °C (τ_1/2 = 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 K_m value compared to that of TMX itself suggested competitive FeP binding to the active site of the host enzyme.

Original language	English
Pages (from-to)	1489-1494
Number of pages	6
Journal	Biomacromolecules
Volume	6
Issue number	3
DOIs	https://doi.org/10.1021/bm049255l
Publication status	Published - 2005 May

ASJC Scopus subject areas

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

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

abstract = "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.",

author = "Teruyuki Komatsu and Seiji Ishihara and Eishun Tsuchida and Hiroyuki Nishide and Chihiro Morokuma and Satoshi Nakamura",

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AU - Ishihara, Seiji

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AU - Nishide, Hiroyuki

AU - Morokuma, Chihiro

AU - Nakamura, Satoshi

PY - 2005/5

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N2 - 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.

AB - 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.

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

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