High-valent intermediates of heme proteins and model compounds.
- Authors
- Type
- Published Article
- Journal
- Current Opinion in Chemical Biology
- Publisher
- Elsevier
- Publication Date
- Dec 01, 2001
- Volume
- 5
- Issue
- 6
- Pages
- 724–735
- Identifiers
- PMID: 11738185
- Source
- Medline
- License
- Unknown
Abstract
Recent computational and experimental probes of high-valent intermediates in heme proteins and model compounds reveal a rich spectrum of chemical behavior that is dependent on the nature of the proximal ligand, metal center, distal- and proximal-binding site environment, porphyrin macrocycle architecture, and consequent electronic structure. The results of such studies reveal an underlying complexity, which is simply understood once one is cognizant of the 'chameleon'-like behavior of such intermediates is determined by the high-valent intermediate environment.