Journal
CHEMICAL SCIENCE
Volume 6, Issue 7, Pages 4060-4065Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5sc01065a
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Funding
- MEXT, Japan [20038784, 26620154, 26288037]
- Yoshida Foundation for Science and Technology
- Swiss National Science Foundation (SNF) [200020_144354]
- NCCR Molecular Systems Engineering
- R'Equip program of the Swiss National Science Foundation (SNF) [316030_145023]
- Grants-in-Aid for Scientific Research [15H01066, 26620154, 15K13743] Funding Source: KAKEN
- Swiss National Science Foundation (SNF) [200020_144354, 316030_145023] Funding Source: Swiss National Science Foundation (SNF)
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As an alternative to Darwinian evolution relying on catalytic promiscuity, a protein may acquire auxiliary function upon metal binding, thus providing it with a novel catalytic machinery. Here we show that addition of cupric ions to a 6-phosphogluconolactonase 6-PGLac bearing a putative metal binding site leads to the emergence of peroxidase activity (k(cat) 7.8 x 10(-2) s(-1), K-M 1.1 x 10(-5) M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme Cu.6-PGLac reveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the o-dianisidine substrate.
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