hemH mutants accumulate all three tetrapyrroles: uroporphyrin, coproporphyrin, and protoporphyrin. Porphyrin accumulation does not occur in these mutants (in a hemA4 background) in the absence of 5-aminolevulinic acid
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structure in presence of iron. Only a single iron ion is found in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron ion is not present in the structure of a His183Ala modified ferrochelatase. Insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264
the three-dimensional structure is determined at 1.9 A resolution by the method of multiple isomorphous replacement. The structural model contains 308 of the 310 amino acid residues of the protein and 198 solvent molecules