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
Waseda Research Institute for Science and Engineering
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.
Biomacromolecules
https://doi.org/10.1021/bm049255l
Endo-1,4-beta Xylanases
Thermodynamic stability
Thermotoga maritima
Xylans
Competitive Binding
Glycoside Hydrolases
(1-4)-xylan
Komatsu, T., Ishihara, S., Tsuchida, E., Nishide, H., Morokuma, C., & Nakamura, S. (2005). Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin. Biomacromolecules, 6(3), 1489-1494. https://doi.org/10.1021/bm049255l
Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin. / Komatsu, Teruyuki; Ishihara, Seiji; Tsuchida, Eishun; Nishide, Hiroyuki; Morokuma, Chihiro; Nakamura, Satoshi.
In: Biomacromolecules, Vol. 6, No. 3, 05.2005, p. 1489-1494.
Komatsu, T, Ishihara, S, Tsuchida, E, Nishide, H, Morokuma, C & Nakamura, S 2005, 'Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin', Biomacromolecules, vol. 6, no. 3, pp. 1489-1494. https://doi.org/10.1021/bm049255l
Komatsu T, Ishihara S, Tsuchida E, Nishide H, Morokuma C, Nakamura S. Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin. Biomacromolecules. 2005 May;6(3):1489-1494. https://doi.org/10.1021/bm049255l
Komatsu, Teruyuki ; Ishihara, Seiji ; Tsuchida, Eishun ; Nishide, Hiroyuki ; Morokuma, Chihiro ; Nakamura, Satoshi. / Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin. In: Biomacromolecules. 2005 ; Vol. 6, No. 3. pp. 1489-1494.
@article{3075fe2c9e3a48f6957a3bc392a4433e,
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",
doi = "10.1021/bm049255l",
journal = "Biomacromolecules",
T1 - Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin
AU - Komatsu, Teruyuki
AU - Ishihara, Seiji
AU - Tsuchida, Eishun
AU - Nishide, Hiroyuki
AU - Morokuma, Chihiro
AU - Nakamura, Satoshi
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.
U2 - 10.1021/bm049255l
DO - 10.1021/bm049255l
JO - Biomacromolecules
JF - Biomacromolecules
10.1021/bm049255l