Synthesis of a cyclic pentapeptide mimic of the active site His-Tyr cofactor of cytochrome c oxidase.
Arylboronic acid based technology provides a mild, regioselective, and nontoxic N-arylation procedure for accessing the unusual N-arylated side chain histidine found in the active site of cytochrome c oxidase (CcO). The N-arylated histidine is elaborated to the complete cytochrome c oxidase cyclic pentapeptide cofactor. Molecular modeling of the cofactor provides insight into the dynamic character of the N-aryl bond.
Mahoney
Maximillian E
ME
Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, USA.
Oliver
Allen
A
Einarsdóttir
Olöf
O
Konopelski
Joseph P
JP
D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008958:Models, Molecular; D018716:Molecular Mimicry; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
D009842:Oligopeptides; D006639:Histidine; D003576:Electron Transport Complex IV; D008239:Lysine