Two electrophoretically distinct forms of superoxide dismutase (SOD; EC 1.15.1.1) which show different inhibition patterns to hydrogen peroxide have been identified in Azotobacter vinelandii. The SOD inhibited by hydrogen peroxide was purified to homogeneity, and turned out to be an iron superoxide dismutase. The enzyme is present in only one molecular form with an isoelectric point of 4.1, and it is composed of two identical subunits with an apparent molecular weight of 21,000 Da. Spectroscopic analyses indicated that this enzyme contains ferric iron (1.4-1.6 mol/mol protein) in the typical high-spin form present in other prokaryotic FeSODs. N-Terminal sequence alignments (up to the 49th residue) showed that A. vinelandii FeSOD has high similarity with other prokaryotic FeSODS.

Purification and characterization of an iron superoxide dismutase from the nitrogen-fixing Azotobacter vinelandii / S. Pagani, R. Colnaghi, A. Palagi, A. Negri. - In: FEBS LETTERS. - ISSN 0014-5793. - 357:1(1995), pp. 79-82.

Purification and characterization of an iron superoxide dismutase from the nitrogen-fixing Azotobacter vinelandii

R. Colnaghi
Secondo
;
A. Negri
Ultimo
1995

Abstract

Two electrophoretically distinct forms of superoxide dismutase (SOD; EC 1.15.1.1) which show different inhibition patterns to hydrogen peroxide have been identified in Azotobacter vinelandii. The SOD inhibited by hydrogen peroxide was purified to homogeneity, and turned out to be an iron superoxide dismutase. The enzyme is present in only one molecular form with an isoelectric point of 4.1, and it is composed of two identical subunits with an apparent molecular weight of 21,000 Da. Spectroscopic analyses indicated that this enzyme contains ferric iron (1.4-1.6 mol/mol protein) in the typical high-spin form present in other prokaryotic FeSODs. N-Terminal sequence alignments (up to the 49th residue) showed that A. vinelandii FeSOD has high similarity with other prokaryotic FeSODS.
Settore BIO/10 - Biochimica
1995
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/182585
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