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Converting Cytochrome c into a Peroxidase‐Like Metalloenzyme by Molecular Design
Author(s) -
Wang ZhongHua,
Lin YingWu,
Rosell Federico I.,
Ni FengYun,
Lu HaoJie,
Yang PengYuan,
Tan XiangShi,
Li XiaoYuan,
Huang ZhongXian,
Mauk A. Grant
Publication year - 2007
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200600547
Subject(s) - cytochrome c peroxidase , peroxidase , heme , hemeprotein , chemistry , horseradish peroxidase , cytochrome c , histidine , enzyme kinetics , cytochrome , cytochrome p450 reductase , stereochemistry , protein design , enzyme , coenzyme q – cytochrome c reductase , biochemistry , protein structure , active site , mitochondrion
Even better than the real thing . Based on molecular design, an electron‐transfer hemoprotein, cytochrome c, was converted into a peroxidase‐like enzyme by introduction of a distal histidine into the heme pocket. The cytochrome c variants obtained, Tyr67His and Tyr67His/Met80Val (see figure), showed much higher peroxidase activities than wild‐type cytochrome protein. More interestingly, the k cat / K m values of the new hemoproteins were higher than that of wild‐type horseradish peroxidase.