Tailor made iron porphyrins for investigating axial ligand and distal environment contributions to electronic structure and reactivity

摘要

Heme proteins catalyse a diverse set of vital life processes using very similar heme cofactor. Thus, the inorganic chemistry community has been investigating factors in the protein active site that control their reactivity. These required synthesis of artificial iron porphyrins where its axial ligand and distal environment were systematically modified. Investigation of the differences in electronic structure and reactivity of these complexes and the intermediates involved in these reactions have revealed striking differences that lead to the diverse reactivity from, apparently, similar looking active site. This review summarises some of these activities in the area of oxygen and nitric oxide activation spanning several decades of dedicated research. (C) 2019 Elsevier B.V. All rights reserved.