Highly efficient catalase activity of metallocorroles

The iron( iii ) complex of a bipolar and amphiphilic corrole, which binds strongly to proteins and undergoes protein-mediated cellular uptake, catalyzes the decomposition of hydrogen peroxide faster ( k cat = 6400 M −1 s −1 ) and more efficiently (turnover frequency >120 s −1 ) than previously re...

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Published inChemical communications (Cambridge, England) Vol. 46; no. 37; pp. 74 - 742
Main Authors Mahammed, Atif, Gross, Zeev
Format Journal Article
LanguageEnglish
Published England 07.10.2010
Subjects
Biocatalysis
Catalase
Catalase - chemistry
Catalase - metabolism
Cellular
Decomposition
Ferric Compounds - chemistry
Hydrogen peroxide
Metalloporphyrins - chemistry
Molecular Structure
Proteins
Uptakes
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Summary:The iron( iii ) complex of a bipolar and amphiphilic corrole, which binds strongly to proteins and undergoes protein-mediated cellular uptake, catalyzes the decomposition of hydrogen peroxide faster ( k cat = 6400 M −1 s −1 ) and more efficiently (turnover frequency >120 s −1 ) than previously reported synthetic compounds with catalase-like activity. The iron( iii ) complex of the bipolar and amphiphilic corrole catalyzes the disproportionation of hydrogen peroxide orders of magnitudes faster and more efficiently than any other synthetic catalytic antioxidant reported to date.
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ISSN:1359-7345
1364-548X
DOI:10.1039/c0cc01989e