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1joa

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{{STRUCTURE_1joa| PDB=1joa | SCENE= }}
{{STRUCTURE_1joa| PDB=1joa | SCENE= }}
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'''NADH PEROXIDASE WITH CYSTEINE-SULFENIC ACID'''
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===NADH PEROXIDASE WITH CYSTEINE-SULFENIC ACID===
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==Overview==
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In order to obtain the crystal structure of the flavoprotein NADH peroxidase with its native Cys42-sulfenic acid redox center, a strategy combining reduced exposure of crystals to ambient oxygen and data collection at -160 degrees C was applied. The structure of the native enzyme to 2.8 A resolution is described; these results conclusively establish the existence of the Cys42-sulfenic acid as the functional non-flavin redox center of the peroxidase and provide the first structure for any naturally occurring protein-sulfenic acid. The Cys42-sulfenic acid atoms C alpha-C beta-S gamma-O roughly define a planar arrangement which is stacked parallel to the si face of the FAD isoalloxazine and positions the sulfenyl oxygen atom only 3.3 A from FAD-C4A. His10-N epsilon 2 contributes a hydrogen bond to the sulfenic acid oxygen, at a distance of 3.2 A. Although one oxygen atom (OX1) of the non-native Cys42-sulfonic acid derivative identified in the earlier wild-type peroxidase structure was taken to represent the native Cys42-sulfenic acid oxygen [Stehle, T., Ahmed, S. A., Claiborne, A., &amp; Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344], this structure shows that the sulfenic acid oxygen does not occupy this position, nor is it hydrogen-bonded to Cys42-N as was OX1. Comparison of the native Cys42-sulfenic acid structure with that of two-electron reduced glutathione reductase provides an insight into the sulfenic acid FAD charge-transfer interaction observed with both wild-type and His10 mutant peroxidases. A model of the E.NADH intermediate recently observed in stopped-flow analyses of the enzyme [Crane, E. J., III, Parsonage, D., Poole, L. B., &amp; Claiborne, A. (1995) Biochemistry 34, 14114-14124] has also been generated to assist in analyzing the chemical mechanism of sulfenic acid reduction.
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(as it appears on PubMed at http://www.pubmed.gov), where 8756456 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8756456}}
==About this Structure==
==About this Structure==
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[[Category: Cysteine-sulfenic acid]]
[[Category: Cysteine-sulfenic acid]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:29:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:32:50 2008''

Revision as of 17:32, 1 July 2008

Image:1joa.png

Template:STRUCTURE 1joa

NADH PEROXIDASE WITH CYSTEINE-SULFENIC ACID

Template:ABSTRACT PUBMED 8756456

About this Structure

1JOA is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.

Reference

Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution., Yeh JI, Claiborne A, Hol WG, Biochemistry. 1996 Aug 6;35(31):9951-7. PMID:8756456

Page seeded by OCA on Tue Jul 1 20:32:50 2008

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