Journal article
Copper(II) Schiff-base complexes and apoglobin stability
Journal of inorganic biochemistry, v 73(3), pp 137-144
1999
PMID: 10331243
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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 π
*-
O-Salprn→d
x
2-y
2
and
N-Salprn→d
x
2-y
2
. 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.
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Details
- Title
- Copper(II) Schiff-base complexes and apoglobin stability
- Creators
- Joseph J. Stephanos - Menoufia UniversityLeia M. Jackson - Drexel UniversityAnthony W. Addison - Drexel University
- Publication Details
- Journal of inorganic biochemistry, v 73(3), pp 137-144
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000080222300003
- Scopus ID
- 2-s2.0-0033104070
- Other Identifier
- 991019168480904721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Chemistry, Inorganic & Nuclear