PMID: 2116319Jul 16, 1990Paper

The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution

FEBS Letters
T StehleG E Schulz

Abstract

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 A (1 A = 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.

References

Jun 5, 1987·Journal of Molecular Biology·P A Karplus, G E Schulz
Jan 1, 1985·Methods in Enzymology·B C Wang
Nov 15, 1981·Journal of Molecular Biology·R ThiemeG E Schulz

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Citations

Jan 15, 1993·European Journal of Biochemistry·T StehleG E Schulz
Oct 1, 2004·The Journal of Biological Chemistry·Argyrides ArgyrouJohn S Blanchard

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