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In vivo incorporation of copper into the iron-exchangeable and manganese-exchangeable superoxide dismutase from Propionibacterium shermanii. Amino acid sequence and identity of the protein moieties.
- Source :
-
European journal of biochemistry [Eur J Biochem] 1994 Jan 15; Vol. 219 (1-2), pp. 463-8. - Publication Year :
- 1994
-
Abstract
- Propionibacterium shermanii, an aerotolerant anaerobe, produces an iron-containing or a manganese-containing superoxide dismutase, depending on the metal supplied in the culture medium [Meier, B., Barra, D., Bossa, F., Calabrese, L. & Rotilio, G. (1982) J. Biol. Chem. 257, 13977-13980]. In this study, we demonstrate in vivo incorporation of copper into an active superoxide-dismutase protein when iron and manganese are absent from the growth medium. Superoxide dismutases containing either iron, manganese or copper were isolated from P. shermanii, their complete amino acid sequences were determined and the identity of their protein moieties was established. The polypeptide chain is made up of 201 amino acid residues, corresponding to a molecular mass of 22.6 kDa. From sedimentation equilibrium experiments, the native protein shows a molecular mass of approximately 86 kDa and therefore consists of four identical subunits. The primary structure was compared with the structure of other Fe-superoxide dismutases and Mn-superoxide dismutases, in particular those possessing a strict metal cofactor specificity.
- Subjects :
- Amino Acid Sequence
Bacteria enzymology
Chromatography, DEAE-Cellulose
Chromatography, Gel
Circular Dichroism
Copper analysis
Kinetics
Molecular Sequence Data
Protein Conformation
Sequence Homology, Amino Acid
Superoxide Dismutase isolation & purification
Copper metabolism
Iron metabolism
Manganese metabolism
Propionibacterium enzymology
Superoxide Dismutase chemistry
Superoxide Dismutase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-2956
- Volume :
- 219
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- European journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 8307013
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1994.tb19960.x