This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1joa
From Proteopedia
|
NADH PEROXIDASE WITH CYSTEINE-SULFENIC ACID
Overview
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 ... [(full description)]
About this Structure
1JOA is a [Single protein] structure of sequence from [Enterococcus faecalis] with FAD as [ligand]. Active as [NADH peroxidase], with EC number [1.11.1.1]. Structure known Active Site: ACT. 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 Oct 30 12:27:13 2007
