Structural aspects of ligand binding to and electron transfer in bacterial and fungal P450s.
Cytochrome P450 enzymes are heme-containing monooxygenases that are named after an absorption band at 450 nm when complexed with carbon monoxide. They catalyze a wide variety of reactions and are unique in their ability to hydroxylate nonactivated hydrocarbons. P450 enzymes are involved in numerous biological processes, which include the biosynthesis of lipids, steroids, antibiotics, and the degradation of xenobiotics. In line with the variety of reactions catalyzed, the size of their substrates varies significantly. Some P450s have open active sites (e.g., BM3), and some have shielded active sites that open only transiently (e.g., P450cam), whereas others bind the substrate only when attached to carrier proteins (e.g., Oxy proteins). Structural aspects of both organic and gaseous ligand binding and electron transfer are described.
Pylypenko
Olena
O
Department of Physical Biochemistry, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany. elena.pylypenko@mpi-dortmund.mpg.de
Schlichting
Ilme
I
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D004579:Electron Transport; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation
D001426:Bacterial Proteins; D005656:Fungal Proteins; D008024:Ligands; D003577:Cytochrome P-450 Enzyme System