Open Access(Hydr)oxo-bridged heme complexes: From structure to reactivity
Author(s) -
María C. Carrasco,
Shabnam Hematian
Publication year - 2019
Publication title -
journal of porphyrins and phthalocyanines
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.322
H-Index - 64
eISSN - 1099-1409
pISSN - 1088-4246
DOI - 10.1142/s1088424619300258
Subject(s) - chemistry , heme , reactivity (psychology) , linker , combinatorial chemistry , hemeprotein , stereochemistry , cofactor , heme a , enzyme , biochemistry , medicine , alternative medicine , pathology , computer science , operating system
Iron–porphyrins ([Formula: see text] hemes) are present throughout the biosphere and perform a wide range of functions, particularly those that involve complex multiple-electron redox processes. Some common heme enzymes involved in these processes include cytochrome P450, heme/copper oxidase or heme/non-heme diiron nitric oxide reductase. Consequently, the (hydr)oxo-bridged heme species have been studied for the important roles that they play in many life processes or for their application for catalysis and preparation of new functional materials. This review encompasses important synthetic, structural and reactivity aspects of the (hydr)oxo-bridged heme constructs that govern their function and application. The properties and reactivity of the bridging (hydr)oxo moieties are directly dictated by the coordination environment of the heme core, the nature and ligation of the second metal center attached to the (hydr)oxo group, the presence or absence of a linker, and the degree of flexibility around that linker within the scaffold. Here, we summarize the structural features of all known (hydr)oxo-bridged heme constructs and use those to categorize and thus, provide a more comprehensive picture of structure–function relationships.