Role of the heme active site and protein environment in structure, spectra, and function of the cytochrome P450s
Article Abstract:
Research into the origin of the low-spin ground state of the ferric resting form of the heme site of cytochrome P450s (CYP450s) is presented. This work also involved considering the properties of the heme site of the substrate-bound ferric species of CYP450s. It is concluded that the electronic structure of the heme unit is well suited to undertake the major functions of heme proteins.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2000
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Peptide-based heme-protein models
Article Abstract:
Research has been conducted on the metalloproteins involved in the fundamental biological processes. The authors review the works on the ability of different proteins to fine-tune the heme cofactor environment to produce different chemistries.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2001
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Heme protein assemblies
Article Abstract:
Approaches to the study of heme proteins are discussed in detail. These studies have demonstrated a number of fundamental concepts in the engineering and construction of metalloproteins.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2004
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