Protocatechuate 3,4‐Dioxygenase

Publisher Website
Google Scholar
Abstract
Cobalt‐containing protocatechuate 3,4‐dioxygenase was purified and crystallized from Pseudomonas aeruginosa which was grown in a medium containing cobalt in place of iron. Although it was indistinguishable from the normal protocatechuate 3,4‐dioxygenase upon ultracentrifugation and acrylamide gel electrophoresis, it had very low enzyme activity compared with the normal enzyme and showed absorption spectra with a shoulder in a region of 420 nm quite different from the normal protocatechuate 3,4‐dioxygenase. It showed distinct electron‐spin resonance signals at g= 4.31 and at g= 2.004. Some other spectral and catalytic properties of the cobalt‐containing protocatechuate 3,4‐dioxygenase were studied and these results indicate the possibility that l‐cysteine residues participate in the ligand of the iron in the active site of the enzyme.

This publication has 15 references indexed in Scilit: