Synthetic Iron Porphyrins as Models for Heme Proteins

Various iron porphyrin complexes have been studied as models for the active sites of heme proteins. Spectroscopic studies of (FeTPP)(,2)N('+) (where TPP is the dianion of tetraphenylporphyrin) and (FeTPP)(,2)C indicate that these complexes contain iron(IV). This behavior can be contrasted with the isoelectronic complex (FeTPP)(,2)O('2+), which contains iron(III) and porphyrin pication radicals. (FePor)(,2)N('+) complexes (where Por can be one of several tetraarylporphyrins) can be further oxidized to yield (FePor)(,2)N('2+), a stable iron(IV) porphyrin pi-cation radical. The electronic structure of these species is dependent on the counterions and porphyrin substituents.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• English, Daniel Roy

• Chemistry, Inorganic

Identifier

(UMI)AAI8502134

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70269