X-ray absorption edge spectroscopy of Co(II)-binding sites of copper- and zinc-containing proteins.
Biochim Biophys Acta
; 670(3): 312-5, 1981 Oct 28.
Article
em En
| MEDLINE
| ID: mdl-6794641
ABSTRACT
X-ray absorption near-edge spectroscopy (XANES) of Co(II) in three derivatives of superoxide dismutase, namely [Cu(II)-Co(II)], [Cu(I)-Co(II)] and [...-Co(II)], suggests a tetrahedral coordination of the metal for all compounds. Significant differences, detected in the spectrum of the [Cu(II)-Co(II)] derivative as compared to the other species, indicate that a conformational change and/or a different charge of the imidazole bridging the two metal sites in superoxide dismutase occur in coincidence with the change of copper valence. The XANES spectra of the cobalt derivatives of alcohol dehydrogenase, carbonic anhydrase and stellacyanin show features that can be accounted for by an increasing degree of covalency in the metal first sphere of coordination, in the following order alcohol dehydrogenase greater than stellacyanin greater than superoxide dismutase greater than or equal to carbonic anhydrase.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Zinco
/
Cobalto
/
Cobre
/
Metaloproteínas
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1981
Tipo de documento:
Article