Copper(II) Schiff-base complexes and apoglobin stability.
N,N'-Propylene-bis-(N-salicylidene)copper(II) (Cu(Salprn)) explicitly stabilizes apomyoglobin. The optical spectrum of this copper(II) Schiff-base complex of apomyoglobin arises from the electronic excitations of pi *-O-Salprn-->dx2-y2 and N-Salprn-->dx2-y2. Shifts of these transitions with respect to those of the parent complex may be a consequence of hydrophobic solvatochromism or binding of an additional ligand. ESR parameters imply no change in the identity of the first coordination sphere around the copper, while hydrophobic solvatochromism cannot be excluded. Combination of copper(II) Schiff-base complex with apomyoglobin does not inhibit the ability of apomyoglobin to extract hemin from the main component of Glycera dibranchiata hemoglobin. Hemin replaces the copper complex, and the value of the apparent first-order rate constant varies with time. The mechanism involves dissociative and associative interchange pathways. Values of rate constants for transfer of hemin to copper(II) Schiff-base apomyoglobin complex, as well as the change of concentration with time are evaluated.
Stephanos
J J
JJ
Chemistry Department, Faculty of Science, El-Menoufia University, Shebin El-Kom, Egypt.
Jackson
L M
LM
Addison
A W
AW
D000818:Animals; D001059:Apoproteins / Q000737:chemistry*; D003300:Copper / Q000737:chemistry; D004355:Drug Stability; D004578:Electron Spin Resonance Spectroscopy; D006427:Hemin / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry; D006736:Horses; D066298:In Vitro Techniques; D009211:Myoglobin / Q000737:chemistry*; D011077:Polychaeta / Q000737:chemistry; D012545:Schiff Bases / Q000737:chemistry
D001059:Apoproteins; D006454:Hemoglobins; D009211:Myoglobin; D012545:Schiff Bases; C010857:apomyoglobin; D006427:Hemin; D003300:Copper