Apocytochrome b5 with a typical heme-binding motif of HPGG, and its variants with mutated motifs, GPGG, GPGH, HVGG, and HPGP, have been subjected to molecular dynamics simulation. Comparison of the dynamic consequence...Apocytochrome b5 with a typical heme-binding motif of HPGG, and its variants with mutated motifs, GPGG, GPGH, HVGG, and HPGP, have been subjected to molecular dynamics simulation. Comparison of the dynamic consequences has revealed the crucial role of HPGG in assembling the heine group of cytochrome b5 and in modulating protein structure, property and function.展开更多
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
基金supported by the initial foundation for Ph.D.introduced into University of South China(No.506XJQ06001).
文摘Apocytochrome b5 with a typical heme-binding motif of HPGG, and its variants with mutated motifs, GPGG, GPGH, HVGG, and HPGP, have been subjected to molecular dynamics simulation. Comparison of the dynamic consequences has revealed the crucial role of HPGG in assembling the heine group of cytochrome b5 and in modulating protein structure, property and function.
基金supported by the National Natural Science Foundation of China,NSFC(No.21101091)Hunan Provincial Natural Science Foundation(No.11JJ4017)+1 种基金Hunan Provincial Education Foundation(No.11B105)the initial foundation for oversea scholar return to University of South China(No.2011XQD16)
文摘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
