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Literature summary extracted from

  • Hansson, M.D.; Karlberg, T.; Rahardja, M.A.; Al-Karadaghi, S.; Hansson, M.
    Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX (2007), Biochemistry, 46, 87-94.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.98.1.1 wild-type and mutants expressed in Escherichia coli BL21(DE3) Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.98.1.1 crystals of wild-type and mutants H183A, H88A and K87A with iron, by addition of solid (NH4)2Fe(SO4)2 x 6 H2O, 1.2 A to 1.7 A resolution Bacillus subtilis
4.98.1.1 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 Bacillus subtilis
4.99.1.9 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 Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
4.98.1.1 E264Q 21% of wild-type activity Bacillus subtilis
4.98.1.1 E264Q activity 21% of wild-type, Kd for Zn(II) is 0.0037 mM Bacillus subtilis
4.98.1.1 E264V less than 1% of wild-type activity Bacillus subtilis
4.98.1.1 E264V activity less than 1% of wild-type Bacillus subtilis
4.98.1.1 H183A less than 1% of wild-type activity Bacillus subtilis
4.98.1.1 H183A almost inactive enzyme, Kd for Zn(II) is 0.015 mM, 4fold decrease in affinity compared to wild-type enzyme Bacillus subtilis
4.98.1.1 H183C less than 1% of wild-type activity Bacillus subtilis
4.98.1.1 H183C Kd for Zn(II) is 0.00064 mM, 6fold increased affinity compared to wild-type Bacillus subtilis
4.98.1.1 H88A 5% of wild-type activity Bacillus subtilis
4.98.1.1 H88A Kd for Zn(II) is 0.0028 mM, activity is 5% of wild-type Bacillus subtilis
4.98.1.1 K87A 92% of wild-type activity Bacillus subtilis
4.98.1.1 K87A retains 92% of wild-type activity, Kd for Zn(II) is 0.013 mM Bacillus subtilis
4.98.1.1 Y13F 71% of wild-type activity Bacillus subtilis
4.98.1.1 Y13F Kd for Zn(II) is 0.0048 mM, Zn(II) bound in a wild-type fashion in the structure Bacillus subtilis
4.99.1.9 E264Q 21% of wild-type activity Bacillus subtilis
4.99.1.9 E264V less than 1% of wild-type activity Bacillus subtilis
4.99.1.9 H183A less than 1% of wild-type activity Bacillus subtilis
4.99.1.9 H183C less than 1% of wild-type activity Bacillus subtilis
4.99.1.9 H88A 5% of wild-type activity Bacillus subtilis
4.99.1.9 K87A 92% of wild-type activity Bacillus subtilis
4.99.1.9 Y13F 71% of wild-type activity Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.98.1.1 Fe2+ single iron in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules Bacillus subtilis
4.98.1.1 Mg2+
-
 Bacillus subtilis
4.98.1.1 Zn2+
-
 Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
4.98.1.1 Bacillus subtilis P32396
-
-
4.98.1.1 Bacillus subtilis 168 P32396
-
-
4.99.1.9 Bacillus subtilis P32396
-
-
4.99.1.9 Bacillus subtilis 168 P32396
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.98.1.1
-
 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.98.1.1 protoporphyrin IX + Fe2+ insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264 Bacillus subtilis ?
-
 ?
4.98.1.1 protoporphyrin IX + Fe2+ insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264 Bacillus subtilis 168 ?
-
 ?