Protein Environment Drives Selectivity for Sulfide Oxidation by an Artificial Metalloenzyme

Magic Mn-salen metallozyme: The design of an original, artificial, inorganic, complex-protein adduct, has led to a better understanding of the synergistic effects of both partners. The exclusive formation of sulfoxides by the hybrid biocatalyst, as opposed to sulfone in the case of the free inorgani...

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Published in:Chembiochem : a European journal of chemical biology 2009-02, Vol.10 (3), p.545-552
Main Authors: Rousselot-Pailley, Pierre, Bochot, Constance, Marchi-Delapierre, Caroline, Jorge-Robin, Adeline, Martin, Lydie, Fontecilla-Camps, Juan C, Cavazza, Christine, Ménage, Stéphane
Format: Article
Language:English
Subjects:
Antioxidants - chemistry
biocatalysis
Catalysis
Chemical Sciences
Circular Dichroism
Ethylenediamines - chemistry
Humans
manganese
metalloenzymes
Metalloproteins - chemistry
Molecular Structure
Organometallic Compounds - chemistry
Oxidation-Reduction
Protein Engineering
protein–metal hybrids
Serum Albumin - chemistry
sulfide oxidation
Sulfides - chemistry
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Summary:Magic Mn-salen metallozyme: The design of an original, artificial, inorganic, complex-protein adduct, has led to a better understanding of the synergistic effects of both partners. The exclusive formation of sulfoxides by the hybrid biocatalyst, as opposed to sulfone in the case of the free inorganic complex, highlights the modulating role of the inorganic-complex-binding site in the protein.Artificial metalloenzymes based on the incorporation of Mn-salen complexes into human serum albumin display high efficiency and selectivity for sulfoxide production during sulfide oxidation. The reactions carried out by the artificial metallozymes are comparable to those carried out by natural biocatalysis. We have found that the polarity of the protein environment is crucial for selectivity and that a synergy between both partners of the hybrid results in the novel activity.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200800595