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Oxidation catalysis by iron and manganese porphyrins within enzyme‐like cages
Author(s) -
Chino Marco,
Leone Linda,
Zambrano Gerardo,
Pirro Fabio,
D'Alonzo Daniele,
Firpo Vincenzo,
Aref Diaa,
Lista Liliana,
Maglio Ornella,
Nastri Flavia,
Lombardi Angela
Publication year - 2018
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.23107
Subject(s) - chemistry , manganese , catalysis , heme , combinatorial chemistry , reactivity (psychology) , cofactor , nanotechnology , organic chemistry , enzyme , materials science , medicine , alternative medicine , pathology
Inspired by natural heme‐proteins, scientists have attempted for decades to design efficient and selective metalloporphyrin‐based oxidation catalysts. Starting from the pioneering work on small molecule mimics in the late 1970s, we have assisted to a tremendous progress in designing cages of different nature and complexity, able to accommodate metalloporphyrins. With the intent of tuning and controlling their reactivity, more and more sophisticated and diverse environments are continuously exploited. In this review, we will survey the current state of art in oxidation catalysis using iron‐ and manganese‐porphyrins housed within designed or engineered protein cages. We will also examine the innovative metal‐organic framework (MOF) systems, exploited to achieving an enzyme‐like environment around the metalloporphyrin cofactor.