2ghc

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{{STRUCTURE_2ghc| PDB=2ghc | SCENE= }}
{{STRUCTURE_2ghc| PDB=2ghc | SCENE= }}
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'''Conformational mobility in the active site of a heme peroxidase'''
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===Conformational mobility in the active site of a heme peroxidase===
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==Overview==
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Conformational mobility of the distal histidine residue has been implicated for several different heme peroxidase enzymes, but unambiguous structural evidence is not available. In this work, we present mechanistic, spectroscopic, and structural evidence for peroxide- and ligand-induced conformational mobility of the distal histidine residue (His-42) in a site-directed variant of ascorbate peroxidase (W41A). In this variant, His-42 binds "on" to the heme in the oxidized form, duplicating the active site structure of the cytochromes b but, in contrast to the cytochromes b, is able to swing "off" the iron during catalysis. This conformational flexibility between the on and off forms is fully reversible and is used as a means to overcome the inherently unreactive nature of the on form toward peroxide, so that essentially complete catalytic activity is maintained. Contrary to the widely adopted view of heme enzyme catalysis, these data indicate that strong coordination of the distal histidine to the heme iron does not automatically undermine catalytic activity. The data add a new dimension to our wider appreciation of structure/activity correlations in other heme enzymes.
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{{ABSTRACT_PUBMED_16762924}}
==About this Structure==
==About this Structure==
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[[Category: Sharp, K H.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:06:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:39:03 2008''

Revision as of 11:39, 29 July 2008

Image:2ghc.png

Template:STRUCTURE 2ghc

Conformational mobility in the active site of a heme peroxidase

Template:ABSTRACT PUBMED 16762924

About this Structure

2GHC is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

Reference

Conformational mobility in the active site of a heme peroxidase., Badyal SK, Joyce MG, Sharp KH, Seward HE, Mewies M, Basran J, Macdonald IK, Moody PC, Raven EL, J Biol Chem. 2006 Aug 25;281(34):24512-20. Epub 2006 Jun 7. PMID:16762924

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