Equilibrium between Fe(iv) porphyrin and Fe(iii) porphyrin radical cation: new insight into the electronic structure of high-valent iron porphyrin complexes

2013 ◽  
Vol 49 (30) ◽  
pp. 3098 ◽  
Author(s):  
Akira Ikezaki ◽  
Masashi Takahashi ◽  
Mikio Nakamura
Keyword(s):  
Electronic Structure ◽  
Radical Cation ◽  
Iron Porphyrin ◽  
Iron Porphyrin Complexes ◽  
High Valent ◽  
Insight Into

High-valent iron-porphyrin complexes related to peroxidase and cytochrome P-450

1981 ◽  
Vol 103 (10) ◽  
pp. 2884-2886 ◽  
Author(s):  
John T. Groves ◽  
Robert C. Haushalter ◽  
Mikio Nakamura ◽  
Thomas E. Nemo ◽  
B. J. Evans
Keyword(s):  
Iron Porphyrin ◽  
Iron Porphyrin Complexes ◽  
High Valent ◽  
Cytochrome P 450

Kinetics of the reduction of iron porphyrin complexes by the methylviologen radical-cation

1987 ◽  
Vol 36 (8) ◽  
pp. 1740-1742
Author(s):  
A. B. Belyaev ◽  
E. I. Karasevich ◽  
V. A. Kuz'min ◽  
P. P. Levin ◽  
A. M. Khenkin
Keyword(s):  
Radical Cation ◽  
Iron Porphyrin ◽  
Reduction Of Iron ◽  
Iron Porphyrin Complexes ◽  
Kinetics Of

Iron porphyrins with a hydrogen bonding cavity: effect of weak interactions on their electronic structure and reactivity

2016 ◽  
Vol 45 (47) ◽  
pp. 18796-18802 ◽  
Author(s):  
Kaustuv Mittra ◽  
Asmita Singha ◽  
Abhishek Dey
Keyword(s):  
Hydrogen Bonding ◽  
Electronic Structure ◽  
Weak Interactions ◽  
Iron Porphyrin ◽  
Iron Porphyrins ◽  
Iron Porphyrin Complexes ◽  
Cavity Effect

The electronic structure and reactivity of iron porphyrin complexes bearing 2nd sphere hydrogen bonding residues have been investigated over the last few years.

Effect of axial ligands on electronic structure and O2 reduction by iron porphyrin complexes: Towards a quantitative understanding of the "push effect"

2015 ◽  
Vol 19 (01-03) ◽  
pp. 92-108 ◽  
Author(s):  
Subhra Samanta ◽  
Pradip Kumar Das ◽  
Sudipta Chatterjee ◽  
Abhishek Dey
Keyword(s):  
Electronic Structure ◽  
Active Sites ◽  
Reduction Reaction ◽  
Axial Ligand ◽  
Iron Porphyrin ◽  
Axial Ligands ◽  
O2 Reduction ◽  
Thiolate Complexes ◽  
Quantitative Understanding ◽  
Iron Porphyrin Complexes

Axial ligands play a dominating role in determining the electronic structure and reactivity of iron porphyrin active sites and synthetic models. Several properties unique to the cysteine bound heme enzyme, cytochrome P450, is attributed to the "push effect" of the thiolate axial ligand. In this mini-review the ground state electronic structure of iron porphyrins with imidazole, phenolate and thiolate complexes, derived using a combination of spectroscopy and DFT calculations, are discussed. The differences in kinetics and selectivity of oxygen reduction reaction (ORR), catalyzed by these iron porphyrin complexes with different axial ligands, help elucidate the varying push effects of the different axial ligands on oxygen activation by ferrous porphyrin. The spectroscopic and kinetic data help to develop a quantitative understanding of the "push effect" and, in particular, the electrostatic and covalent contributions to it.

Aliphatic hydroxylation catalyzed by iron porphyrin complexes

1983 ◽  
Vol 105 (20) ◽  
pp. 6243-6248 ◽  
Author(s):  
John T. Groves ◽  
Thomas E. Nemo
Keyword(s):  
Iron Porphyrin ◽  
Iron Porphyrin Complexes
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