New Understanding over Catalytic Mechanism of Iron-Heme System Based Oxidases
WANG Zhi-Peng1,2, YUAN Jin-Ying1
1. Department of Chemistry, Tsinghua University, Beijing 100084, China;
2. Department of Chemistry, Texas A & M University, College Station, TX, 77840, USA
Abstract Iron-heme is the active center of many vital oxidases in life systems. The porphyrin, as a conjugated ligand with a large aromatic ring structure, has more complicated coordination interactions than normal small molecular ligands. The mechanistic studies showed the existence of multiple positively charged or free radical iron-oxo species in the oxidation process. Their corresponding structures and the changes in the oxidation state of the center iron atom are hard to describe simply using traditional Valence Bond Theory (VBT) or Valence-Shell Electron-Pair Repulsion Theory(VSEPR). Additionally, the formation of the core intermediates varies in different enzymes. This paper provides some new understanding over several mechanism-related questions, hoping to contribute to the education and research of bioinorganic chemistry, coordination chemistry, bioorganic chemistry, and enzymology.
WANG Zhi-Peng, YUAN Jin-Ying. New Understanding over Catalytic Mechanism of Iron-Heme System Based Oxidases[J]. Chinese Journal of Chemical Education, 2016, 37(12): 4-7.
