摘要
By retaining the native distal His64 in sperm whale myoglobin （Mb）, a second distal histidine was engineered in Mb by mutating Leu29 to His29. The resultant mutant of L29H Mb exhibits an unusual enhanced peroxidase activity with a positive cooperativity in comparison to that of wild type Mb. The new enzyme with two cooperative distal histidines has not been found in native peroxidase, which emohasizes a creation of the rational nmt^in doclan
By retaining the native distal His64 in sperm whale myoglobin （Mb）, a second distal histidine was engineered in Mb by mutating Leu29 to His29. The resultant mutant of L29H Mb exhibits an unusual enhanced peroxidase activity with a positive cooperativity in comparison to that of wild type Mb. The new enzyme with two cooperative distal histidines has not been found in native peroxidase, which emohasizes a creation of the rational nmt^in doclan
基金
supported by the National Natural Science Foundation of China,NSFC(No.21101091)
Hunan Provincial Natural Science Foundation(No.11JJ4017)
Hunan Provincial Education Foundation(No.11B105)
the initial foundation for oversea scholar return to University of South China(No.2011XQD16)
