2e2y
From Proteopedia
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Crystal Structure of F43W/H64D/V68I Myoglobin
Overview
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.
About this Structure
2E2Y is a Single protein structure of sequence from Physeter catodon with , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:05:29 2008
Categories: Physeter catodon | Single protein | Hikage, T. | Ohki, T. | Suzuki, A. | Ueno, T. | Watanabe, Y. | Yamane, T. | GOL | HEM | SO4 | Oxygen storage/transport
