High-valent intermediates of heme proteins and model compounds.
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.
Harris
D L
DL
Molecular Research Institute, Mountain View, California 94043, USA. dannil@purisima.molres.org
D002374:Catalase / Q000737:chemistry*; D002711:Chloride Peroxidase / Q000737:chemistry*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D006420:Hemeproteins / Q000737:chemistry*; D007501:Iron / Q000737:chemistry; D008345:Manganese / Q000737:chemistry; D008958:Models, Molecular; D011789:Quantum Theory
D006420:Hemeproteins; D008345:Manganese; D003577:Cytochrome P-450 Enzyme System; D007501:Iron; D002711:Chloride Peroxidase; D002374:Catalase