The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution |
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| Authors: | T Stehle S A Ahmed A Claiborne G E Schulz |
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| Affiliation: | Institut für Organische Chemie und Biochemie, Freiburg, FRG. |
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| 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. |
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