Hydrogen-Bonding Interactions Trigger a Spin-Flip in Iron(III) Porphyrin Complexes

Overview

Journal Angew Chem Weinheim Bergstr Ger

Date 2015 Jun 26

PMID 26109743

Citations 2

Authors

Dipankar Sahoo

Matthew G Quesne

Sam P de Visser

Sankar Prasad Rath

Affiliations

Soon will be listed here.

Abstract

A key step in cytochrome P450 catalysis includes the spin-state crossing from low spin to high spin upon substrate binding and subsequent reduction of the heme. Clearly, a weak perturbation in P450 enzymes triggers a spin-state crossing. However, the origin of the process whereby enzymes reorganize their active site through external perturbations, such as hydrogen bonding, is still poorly understood. We have thus studied the impact of hydrogen-bonding interactions on the electronic structure of a five-coordinate iron(III) octaethyltetraarylporphyrin chloride. The spin state of the metal was found to switch reversibly between high (S=/) and intermediate spin (S=/) with hydrogen bonding. Our study highlights the possible effects and importance of hydrogen-bonding interactions in heme proteins. This is the first example of a synthetic iron(III) complex that can reversibly change its spin state between a high and an intermediate state through weak external perturbations.

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