Significant interaction between low-spin iron(III) site and pyrroloquinoline quinone in active center of nitrile hydratase.
Nitrile hydratase, a unique non-heme iron enzyme, contains low-spin Fe(III) site and pyrroloquinoline quinone in the active center. The enzymatic activity of nitrile hydratase is strongly inhibited by typical carbonyl reagents such as phenylhydrazine and semicarbazide. Of special interest is the fact that these carbonyl reagents induced significant alteration of the ESR features of the native iron(III) enzyme at pH 7.2. In addition, the isobutyronitrile(inhibitor)-bound enzyme was also remarkably affected by phenylhydrazine and then the transformed ESR characteristics were different from those of phenylhydrazine-treated enzyme. The present results reveal the first evidence for an important interaction between the low-spin Fe(III) site and pyrroloquinoline quinone which is essential for the activity of nitrile hydratase.
Sugiura
Y
Y
Institute for Chemical Research, Kyoto University, Japan.
Kuwahara
J
J
Nagasawa
T
T
Yamada
H
H
D001665:Binding Sites; D001951:Brevibacterium / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy; D005290:Ferric Compounds / Q000378:metabolism*; D006836:Hydro-Lyases / Q000378:metabolism*; D008433:Mathematics; D045542:PQQ Cofactor; D011549:Pseudomonas / Q000201:enzymology; D011804:Quinolines / Q000378:metabolism*
D005290:Ferric Compounds; D011804:Quinolines; D045542:PQQ Cofactor; D006836:Hydro-Lyases; C048831:nitrile hydratase