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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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 (O(2)) in aqueous medium (pH 7.3, 25 degrees C) in the same manner as hemoglobin and myoglobin. The oxygenated species was sufficiently stable; the half-lifetime against the ferric state (tau(1/2)) was 5 h. This O(2)-carrying hemoprotein showed a high degree of thermal stability over a wide range of temperatures up to 90 degrees C (tau(1/2) = 5 min at 90 degrees C and 9 min at 75 degrees C). Dictyoglomus thermophilum xylanase B (DTX; family G/11) also incorporates FeP, and DTX-FeP showed identical O(2)-binding parameters and thermostability. TMX-FeP is capable of catalyzing the beta-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.[1]

References

  1. Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic iron(II) porphyrin. Komatsu, T., Ishihara, S., Tsuchida, E., Nishide, H., Morokuma, C., Nakamura, S. Biomacromolecules (2005) [Pubmed]
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