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| {{STRUCTURE_1oaf| PDB=1oaf | SCENE= }} | | {{STRUCTURE_1oaf| PDB=1oaf | SCENE= }} |
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| '''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE'''
| | ===ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE=== |
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| ==Overview==
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| Heme peroxidases catalyze the H2O2-dependent oxidation of a variety of substrates, most of which are organic. Mechanistically, these enzymes are well characterized: they share a common catalytic cycle that involves formation of a two-electron, oxidized Compound I intermediate followed by two single-electron reduction steps by substrate. The substrate specificity is more diverse--most peroxidases oxidize small organic substrates, but there are prominent exceptions--and there is a notable absence of structural information for a representative peroxidase-substrate complex. Thus, the features that control substrate specificity remain undefined. We present the structure of the complex of ascorbate peroxidase-ascorbate. The structure defines the ascorbate-binding interaction for the first time and provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis for more than 20 years. A new mechanism for electron transfer is proposed that challenges existing views of substrate oxidation in other peroxidases.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12640445}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12640445 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12640445}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Heme peroxidase]] | | [[Category: Heme peroxidase]] |
| [[Category: Peroxide scavenge]] | | [[Category: Peroxide scavenge]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:35:41 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:35:35 2008'' |
