Formation and spectroscopic characterization of the dioxygen adduct of a heme-Cu complex possessing a cross-linked tyrosine-histidine mimic: modeling the active site of cytochrome c oxidase.
A binucleating porphyrin with covalently appended copper chelates having a cross-linked imidazole-phenol group as the novel active site model of cytochrome c oxidase has been prepared, and the dioxygen adduct of its iron(II)-copper(I) complex was spectroscopically characterized.
Liu
Jin-Gang
JG
Institute for Materials Chemistry and Engineering, Kyushu University, Higashi-ku, Fukuoka 812-8581, Japan.
Naruta
Yoshinori
Y
Tani
Fumito
F
Chishiro
Takefumi
T
Tachi
Yoshimitsu
Y
D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D003576:Electron Transport Complex IV / Q000737:chemistry*; D006418:Heme / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D007093:Imidazoles / Q000737:chemistry; D018716:Molecular Mimicry; D015394:Molecular Structure; D010100:Oxygen / Q000737:chemistry*; D010636:Phenols / Q000737:chemistry; D011166:Porphyrins / Q000032:analysis / Q000737:chemistry; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman / Q000379:methods; D014443:Tyrosine / Q000737:chemistry*
D007093:Imidazoles; D010636:Phenols; D011166:Porphyrins; D014443:Tyrosine; D006418:Heme; D006639:Histidine; D003300:Copper; C029899:imidazole; D003576:Electron Transport Complex IV; D010100:Oxygen