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| Unusual peroxidase activity of a myoglobin mutant with two distal histidines |
| Wei Wei Guo a, Dun Wan a, Li Fu Liao a, Ying Wu Lin a, b, * |
a School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China
b State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing 210093, China |
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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.
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