Reaction route control by microperoxidase-9/CTAB micelle ratios

Physical Chemistry Chemical Physics : PCCP
Tatiana PrietoIseli L Nantes

Abstract

Microperoxidases (MP) as water-soluble models attract interest to studying the reaction mechanism of peroxidases because these heme peptides are able to form the same enzyme intermediates during the reaction with peroxides. In this work we have demonstrated that the association of Fe(III)MP-9 and Fe(III)MP-11 with CTAB micelles (MP-9/CTAB and MP11/CTAB) provides a microenvironment with an alkaline interface and a hydrophobic core that exhibits peroxidase behavior. This microenvironment shifts positively the redox potential of microperoxidases by approximately 100 mV. tert-Butylhydroperoxide (t-BuOOH) when added to the medium, converted Fe(III)MP-9/CTAB to MP-9/CTAB Compound II, a high valence oxidized intermediate of the heme peptide. Subsequent addition of diphenylacetaldehyde (DPAA) to MP-9/CTAB Compound II regenerated the native form of the enzyme, Fe(III)MP-9/CTAB, what characterizes the occurrence of a peroxidase cycle. Fe(III)MP-9/CTAB regenerated during the peroxidase cycle reacted with residual DPAA in the medium to form Fe(II)MP-9/CTAB, which indicates that both Fe(III)MP-9/CTAB and its oxyferryl form can use aldehydes as reducing agents. According to the determined reduction potential, Fe(III)MP-9 and Fe(III)MP-9/CTAB...Continue Reading

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Citations

Sep 26, 2013·Chemical Research in Toxicology·Thiago C Genaro-MattosSayuri Miyamoto
Jul 5, 2011·Biochemical Pharmacology·Marzena Poraj-KobielskaMartin Hofrichter
Sep 22, 2015·Frontiers in Molecular Biosciences·Ana M Carmona-RibeiroIseli L Nantes
Jan 28, 2016·Physical Chemistry Chemical Physics : PCCP·Taegon LeeManho Lim
Sep 22, 2017·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Tatiana PrietoIseli L Nantes-Cardoso
Apr 25, 2021·Journal of Inorganic Biochemistry·Virginia DizSara E Bari

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