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The structure of NADH peroxidase from Streptococcus faecalis at 3.3 Å resolution
Author(s) -
Stehle T.,
Ahmed S.A.,
Claiborne A.,
Schulz G.E.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80921-5
Subject(s) - tetramer , chemistry , oxidoreductase , stereochemistry , peroxidase , glutathione reductase , crystallography , biochemistry , reductase , monomer , enzyme , glutathione , glutathione peroxidase , organic chemistry , polymer
NADH peroxidase (EC 1.11.1.1) previously isolated from Streptococcus faecalis 10C1 has been crystallized. The crystal structure has been solved by multiple isomorphous replacement and solvent‐flattening at 3.3 Å (1 Å = 0.1 nm) resolution. The enzyme forms a tetramer consisting of 4 crystallographically related subunits. The monomer chain fold is in general similar to those of glutathione reductase and lipoamide dehydrogenase. FAD binds in the same region and in a similar conformation as in glutathione reductase. The unusual cysteine‐sulfenic acid participating in catalysis is located at the isoalloxazine of FAD.