2e2y

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(New page: 200px<br /><applet load="2e2y" size="350" color="white" frame="true" align="right" spinBox="true" caption="2e2y, resolution 1.60&Aring;" /> '''Crystal Structure of...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: oxygen storage/transport]]
[[Category: oxygen storage/transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:41:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:05:29 2008''

Revision as of 15:05, 21 February 2008

Image:2e2y.jpg

2e2y, resolution 1.60Å

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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

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