Journal:JBIC:4
From Proteopedia
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| - | <applet load="2l0u" size="600" color="" frame="true" spin="on" Scene ="Journal:JBIC:4/Heme_bound_ferro_open/ | + | <applet load="2l0u" size="600" color="" frame="true" spin="on" Scene ="Journal:JBIC:4/Heme_bound_ferro_open/3" align="right" caption="Solved Crystal Structure of Ferrochelatase Mutant"/> |
=== Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase === | === Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase === | ||
<big>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</big> | <big>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</big> | ||
Revision as of 11:00, 31 October 2010
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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 ferrochelatases 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.
