Journal:JBIC:4
From Proteopedia
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Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase
Mattias D. Hansson • Tobias Karlberg • Christopher A. G. So ̈derberg • Sreekanth Rajan • 5 Martin J. Warren • Salam Al-Karadaghi • Stephen E. J. Rigby • Mats Hansson
Molecular Tour
Ferrochelatase produces . It can also . However, the ability to insert other metal ions is species specific. In this way Bacillus subtilis ferrochelatase can insert copper,. In contrast, the human and Saccharomyces cerevisiae prefer cobalt over copper. . A third residue, is a third ligand via a water molecule. In the structures of the ferrochelatases the Tyr/Met occupies the same position. We also know that the Tyr residue of the B. subtilis enzyme is a direct ligand to a copper-porphyrin reaction product. By site directed mutagenesis we changed the Tyr to a Met residue and showed that the metal specificity changed so that the modified B. subtilis ferrochelatase preferred cobalt over copper. Two Proteopedia structures are presented. One shows how . The other shows how a in the B. subtilis enzyme.
