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.

Role of 2nd sphere H-bonding residues in tuning the kinetics of CO2 reduction to CO by iron porphyrin complexes

2019 ◽  
Vol 48 (18) ◽  
pp. 5965-5977 ◽  
Author(s):  
Pritha Sen ◽  
Biswajit Mondal ◽  
Dibyajyoti Saha ◽  
Atanu Rana ◽  
Abhishek Dey
Keyword(s):  
Co2 Reduction ◽  
Iron Porphyrin ◽  
Iron Porphyrins ◽  
Iron Porphyrin Complexes ◽  
Kinetics Of

A series of iron porphyrins that vary only in the distal H-bonding network exhibit turnover frequencies (TOFs) ranging from 1.0 s−1 to 103 s−1.

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

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

scholarly journals Calculation of Higher Protonation States and of a New Resting State for Vanadium Chloroperoxidase Using QM/MM, with an Atom-in-Molecules Analysis

2020 ◽  
Author(s):  
Gregory Anderson ◽  
Raghu Nath Behera ◽  
Ravi V. Gomatam
Keyword(s):  
Hydrogen Bonding ◽  
Electronic Structure ◽  
Resting State ◽  
Natural Bond Orbital ◽  
Atoms In Molecules ◽  
Aim Analysis ◽  
Neutral Ph

<p></p><p><b>ABSTRACT</b>. <a></a><a></a><a>Earlier QM/MM studies of the resting state of vanadium chloroperoxidase (VCPO) focused on the diprotonated states of the vanadate cofactor. Herein, we report a new extensive QM/MM study that includes the tri- and quadprotonated states of VCPO at neutral pH. We identify certain di- and triprotonated states as being candidates for the resting state based on a comparison of relative energies. The quadprotonated states as well as some of the triprotonated states are ruled out as the resting state. An Atoms-in-Molecules (AIM) analysis of the complex hydrogen bonding around the vanadate cofactor helps to explain the relative energies of the protonation states considered herein, and it also indicates new hydrogen bonding which has not been recognized previously. A Natural Bond Orbital (NBO) study is presented to give a better understanding of the electronic structure of the vanadate co-factor.</a></p><br><p></p>

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