Cytochrome P-450 modelling oxygenation of olefins within the space-restricted cavity of iron “binap porphyrin”: Rate enhancement in the presence of imidazole-Reference-Cited by-同舟云学术

Cytochrome P-450 modelling oxygenation of olefins within the space-restricted cavity of iron “binap porphyrin”: Rate enhancement in the presence of imidazole

Published:1987-01 Issue:39 Volume:28 Page:4553-4556
ISSN:0040-4039
Container-title:Tetrahedron Letters
language:en
Short-container-title:Tetrahedron Letters

Author:

Naruta Yoshinori,Maruyama Kazuhiro

Publisher

Elsevier BV

Subject

Organic Chemistry,Drug Discovery,Biochemistry

Reference14 articles.

1. The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.

2. Dynamics of axial ligation in metalloporphyrins. I. Imidazole exchange in low-spin ferric porphyrins

3. Equilibriums of imidazole with iron(III) tetraphenylporphine

4. Electronic effects in transition metal porphyrins. The reactions of imidazoles and pyridines with a series of para-substituted tetraphenylporphyrin complexes of chloroiron(III)

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1. Iron and manganese (III) porphyrin covalently bound to poly(acryloyl chloride) as biomimetic heterogeneous catalysts for alkene epoxidation by NaIO4: advantage of iron (III) porphyrin and significance of nitrogen donor axial ligands;Journal of the Iranian Chemical Society;2015-09-02

2. Investigation of axial ligand effects on catalytic activity of manganese porphyrin, evidence for the importance of hydrogen bonding in cytochrome-P450 model reactions;Journal of Porphyrins and Phthalocyanines;2014-05

3. Crystal structure of a chiral binaphthyl porphyrin;Journal of Porphyrins and Phthalocyanines;2012-03

4. Corrigendum to “Comparison between the two different forms of iron(IV)-oxo porphyrin and the effects of neutral axial ligand on their catalysis: A theoretical study” [Comput. Theor. Chem. 966 (2011) 62–69];Computational and Theoretical Chemistry;2011-08

5. Water increases rates of epoxidation by Mn(iii)porphyrins/imidazole/IO4− in CH2Cl2. Analogy with peroxidase and chlorite dismutase;Dalton Transactions;2011