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 • 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 . In this way Bacillus subtilis ferrochelatase can , but to a much less extent cobalt. In contrast, the human and Saccharomyces cerevisiae ferrochelatases . Our structural work shows that . A third residue, Tyr in B. subtilis ferrochelatase and 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 is a . 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 crystal structures are presented. how . The how a in the B. subtilis enzyme.
