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J. Biol. Chem., Vol. 268, Issue 12, 8541-8546, 04, 1993
A Abbas and R Labbe-Bois
The molecular basis of the ferrochelatase defects was investigated in two
"protoporphyric" and partially heme-deficient yeast mutants.
Ferrochelatase, a mitochondrial inner membrane-bound enzyme, catalyzes the
incorporation of ferrous iron into protoporphyrin, the last step in
protoheme biosynthesis. The mutant cells made normal amounts of normal-
sized ferrochelatase, as detected by immunoblotting. The mutations were
identified by sequencing the mutant hem15 alleles amplified in vitro from
mutant strains genomic DNA. A single nucleotide change, causing an amino
acid substitution, was found in each mutant. Substitution of the conserved
Ser-169 by Phe caused a 10-fold increase in Vmax and a 45- and 35-fold
increase in the KM for protoporphyrin and metal, respectively. Replacement
of Ser-174 by Pro produced the same effects, but to a lesser degree. There
was a good correlation between the ferrochelatase defects measured in vitro
and the heme synthesis deficiencies estimated in vivo. The decreased in
vivo heme synthesis is probably due to the lower affinity of the mutant
enzymes for iron. We propose that the region identified by the two close
mutations contributes to the binding domains of metal and protoporphyrin.
Structure-function studies of yeast ferrochelatase. Identification and functional analysis of amino acid substitutions that increase Vmax and the KM for both substrates
Laboratoire de Biochimie des Porphyrines, Institut Jacques Monod, Universite Paris 7, France.
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