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Unusual peroxidase activity of a myoglobin mutant with two distal histidines 被引量:3
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作者 Wei Wei Guo dun wan +1 位作者 Li Fu Liao Ying Wu Lin 《Chinese Chemical Letters》 SCIE CAS CSCD 2012年第6期741-744,共4页
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 ... 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 展开更多
关键词 Heme protein MYOGLOBIN Protein design PEROXIDASE COOPERATIVITY
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