Short communicationRemarkable axial thiolate ligand effect on the oxidation of hydrocarbons by active intermediate of iron porphyrin and cytochrome P450
Section snippets
Acknowledgements
This work was supported in part by a Grant-in-Aid for Scientific Research (No. 07407079, Biometallics No. 10129203 and No. 11116207) from the Ministry of Education, Science, Sports and Culture, Japan.
References (10)
- et al.
Biochem. Biophys. Res. Commun.
(1978) - et al.
Chem. Rev.
(1996) - et al.
FASEB J.
(1990) - et al.
J. Am. Chem. Soc.
(1990) - et al.
J. Am. Chem. Soc.
(1993)
Cited by (53)
Diheme cytochromes: Effect of mixed-axial ligation on the electronic structure and electrochemical properties with cobalt porphyrin dimer
2023, Journal of Inorganic BiochemistryIron and manganese biomimetic compounds
2021, Comprehensive Coordination Chemistry IIIMechanistic studies on versatile metal-assisted hydrogen peroxide activation processes for biomedical and environmental incentives
2016, Coordination Chemistry ReviewsRedox cycling in the activation of peroxides by iron porphyrin and manganese complexes. 'Catching' catalytic active intermediates
2016, Coordination Chemistry ReviewsCitation Excerpt :A significant source of knowledge, improving comprehension of the formation and oxygenation capability of intermediates postulated as reactive agents responsible for substrate conversion by heme enzymes, came from experimental and theoretical studies with the application of synthetic porphyrin models [20–23]. Particular attention was devoted to the elucidation of structures of reactive intermediates, as well as the nature of OO bond activation occurring in catalytic oxygenation reactions conducted by heme enzymes in reactions with various oxidants [24–55]. The differences in catalytic ability of heme enzymes and the variety of catalyzed reactions are ascribed to dissimilarities of the prosthetic group, the nature of the heme environment, and the steric accessibility of the heme iron.
Effect of imidazole on biomimetic cyclohexane oxidation by first-, second-, and third-generation manganese porphyrins using PhIO and PhI(OAc)<inf>2</inf> as oxidants
2015, Applied Catalysis A: GeneralCitation Excerpt :The second region refers to the prosthetic group heme, composed of an ironprotoporphyrin IX axially coordinated to sulfur atoms of amino acid residues with a free site for subsequent molecular oxygen activation [27]. The presence of this axial ligand is believed to affect the reactivity of these catalysts directly, boosting product yields and selectivity during alkanes CH bond hydroxylation reactions [28]. To assess the axial ligand effect, various researchers have developed biomimetic systems based on the combination of iron or manganese porphyrins and pyridine or imidazole as axial ligands.