1dcc

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[[Image:1dcc.gif|left|200px]]
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{{Seed}}
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[[Image:1dcc.png|left|200px]]
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{{STRUCTURE_1dcc| PDB=1dcc | SCENE= }}
{{STRUCTURE_1dcc| PDB=1dcc | SCENE= }}
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'''2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX'''
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===2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX===
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==Overview==
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The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one proton from the transient Fe+3-OOH complex. We therefore determined the crystal structure of the Fe+2-O2 complex formed by a yeast cytochrome c peroxidase mutant with Trp 191 replaced by Phe. The refined structure shows that dioxygen can form a hydrogen bond with the conserved distal His residue, but not with the conserved distal Arg residue. When the transient Fe+3-OOH complex is modelled in a similar orientation, the active site of peroxidase appears to be optimized for catalysing proton transfer between the vicinal oxygen atoms of the peroxy-anion.
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The line below this paragraph, {{ABSTRACT_PUBMED_7664080}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 7664080 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7664080}}
==About this Structure==
==About this Structure==
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[[Category: Miller, M A.]]
[[Category: Miller, M A.]]
[[Category: Shaw, A.]]
[[Category: Shaw, A.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:41:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:48:59 2008''

Revision as of 19:49, 30 June 2008

Template:STRUCTURE 1dcc

2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX

Template:ABSTRACT PUBMED 7664080

About this Structure

1DCC is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex., Miller MA, Shaw A, Kraut J, Nat Struct Biol. 1994 Aug;1(8):524-31. PMID:7664080

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