Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution

J Mol Biol. 1991 Oct 20;221(4):1325-44.


The crystal structure of NADH peroxidase (EC from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been refined to a resolution of 2.16 A using the simulated annealing method. The final crystallographic R-factor is 17.7% for all data in the resolution range 7 to 2.16 A. The standard deviations are 0.015 A in bond lengths and 3.0 degrees in bond angles for the final model, which includes all 447 amino acid residues, one FAD and 369 water molecules. The enzyme is a symmetrical tetramer with point group D2; the symmetry is crystallographic. The redox center of the enzyme consists of FAD and a cysteine (Cys42), which forms a sulfenic acid (Cys-SOH) in its oxidized state. A histidine (His10) close to Cys42 is likely to act as an active-site base. In the analyzed crystal, the enzyme was in a non-native oxidation state with Cys42 oxidized to a sulfonic acid Cys-SO3H. The chain fold of NADH peroxidase is similar to those of disulfide oxidoreductases. A comparison with glutathione reductase, a representative of this enzyme family, is given.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites / physiology
  • Crystallization
  • Cysteic Acid / chemistry
  • Enterococcus faecalis / enzymology*
  • Glutathione Reductase / chemistry
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Peroxidases / chemistry*
  • Peroxidases / isolation & purification
  • Protein Conformation
  • X-Ray Diffraction


  • Macromolecular Substances
  • Cysteic Acid
  • Peroxidases
  • NAD+ peroxidase
  • Glutathione Reductase