Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties.
1. The aim of the present work is to shed light on the way of action of hexachlorobenzene (HCB) on hepatic ferrochelatase the mitochondrial enzyme which catalyzes the last step of haem biosynthetic pathway. 2. Some properties of this enzyme from normal and HCB porphyric rat liver were studied. 3. The present findings indicate that HCB treatment would modify the configuration of the enzyme perhaps allowing the active center of the porphyric ferrochelatase to be more exposed. 4. As a consequence it would show: (a) its higher affinity for the iron; (b) the shorter time necessary to form the intermediate enzyme-substrate, reflected both by the existence of a shorter lag and consequently a shorter pre incubation time. 5. However this modification elicited by the fungicide does not alter the submitochondrial distribution of the enzyme nor the optimal conditions for its measurement.
Rios de Molina
M C
MC
Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina.
Taira
M C
MC
San Martin de Viale
L C
LC
D000818:Animals; D002722:Chlorobenzenes / Q000494:pharmacology*; D004795:Enzyme Stability; D005294:Ferrochelatase / Q000378:metabolism*; D006418:Heme / Q000096:biosynthesis; D006581:Hexachlorobenzene / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D008190:Lyases / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology*; D011164:Porphyrias / Q000139:chemically induced / Q000201:enzymology*; D051381:Rats
D002722:Chlorobenzenes; D006418:Heme; D006581:Hexachlorobenzene; D008190:Lyases; D005294:Ferrochelatase