Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1257482 | Chinese Chemical Letters | 2012 | 4 Pages |
Abstract
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 emphasizes a creation of the rational protein design.
Related Topics
Physical Sciences and Engineering
Chemistry
Chemistry (General)
Authors
Wei Wei Guo, Dun Wan, Li Fu Liao, Ying Wu Lin,