Unusual peroxidase activity of a myoglobin mutant with two distal histidines  

作　　者：Wei Wei Guo Dun Wan Li Fu Liao Ying Wu Lin 

机构地区：[1]School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China [2]State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing 210093, China

出　　处：《Chinese Chemical Letters》2012年第6期741-744,共4页中国化学快报（英文版）

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)

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 doclanBy 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

关 键 词：Heme protein MYOGLOBIN Protein design PEROXIDASE COOPERATIVITY 

分 类 号：Q554.6[生物学—生物化学] Q51