Kinetic studies of ferrochelatase in yeast. Zinc or iron as competing substrates.
Ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) has been studied in yeast mitochondrial membranes with special reference to zinc-chelatase and iron-chelatase activities. Using physiological substrates (protoporphyrin IX, Fe(II) and Zn(II), anaerobic conditions of incubation and direct spectrophotometric assay, apparent Km values smaller than those previously described were found for the membrane-bound enzyme. Fe(II) but not Fe(III) was a strong competitive inhibitor of zinc-chelatase activity, while Zn(II) was a slight competitive inhibitor of iron-chelatase activity. These results could point to modes of control of ferrochelatase activity in yeast. We suggest that reduced supply of Fe(II) may explain the in vivo accumulation of zinc-protoporphyrin in yeast cells incubated under 'resting' conditions.
D000693:Anaerobiosis; D005294:Ferrochelatase / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D008190:Lyases / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D015032:Zinc / Q000378:metabolism*
D007501:Iron; D008190:Lyases; D005294:Ferrochelatase; D015032:Zinc