Abstract

Abstract We have determined the crystal structure of thermoglobin (AaTgb) from a hyperthermophilic bacterium Aquifex aeolicus. Tyrosine and glutamine at the B10 and E7 position, respectively, are conserved in AaTgb as are the case of single domain hemoglobins (sdHbs). While the binding affinity of O2 or CO is affected by the replacement of Tyr29 in the distal heme pocket, wild type and Y29F variant of AaTgb show a similar binding affinity of imidazole.

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