Structural highlights
Function
MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A series of myoglobin mutants, in which distal sites are modified by site-directed mutagenesis, are able to catalyze peroxidase, catalase, and P450 reactions even though their proximal histidine ligands are intact. More importantly, reactions of P450, catalase, and peroxidase substrates and compound I of myoglobin mutants can be observed spectroscopically. Thus, detailed oxidation mechanisms were examined. On the basis of these results, we suggest that the different reactivities of P450, catalase, and peroxidase are mainly caused by their active site structures, but not the axial ligand. We have also prepared compound 0 under physiological conditions by employing a mutant of cytochrome c 552. Compound 0 is not able to oxidize ascorbic acid.
Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants.,Watanabe Y, Nakajima H, Ueno T Acc Chem Res. 2007 Jul;40(7):554-62. Epub 2007 Jun 14. PMID:17567089[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Watanabe Y, Nakajima H, Ueno T. Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants. Acc Chem Res. 2007 Jul;40(7):554-62. Epub 2007 Jun 14. PMID:17567089 doi:10.1021/ar600046a
