2e2y

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Revision as of 10:41, 23 January 2008

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spinqualitylabelsall models 2e2y, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

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