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Investigation of the highly active manganese superoxide dismutase from Saccharomyces cerevisiae

Title
Investigation of the highly active manganese superoxide dismutase from Saccharomyces cerevisiae
Authors
Barnese K.Sheng Y.Stich T.A.Gralla E.B.David Britt R.Cabelli D.E.Valentine J.S.
Ewha Authors
Joan S. Valentine
SCOPUS Author ID
Joan S. Valentinescopus
Issue Date
2010
Journal Title
Journal of the American Chemical Society
ISSN
0002-7863JCR Link
Citation
vol. 132, no. 36, pp. 12525 - 12527
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Manganese superoxide dismutase (MnSOD) from different species differs in its efficiency in removing high concentrations of superoxide (O 2 -), due to different levels of product inhibition. Human MnSOD exhibits a substantially higher level of product inhibition than the MnSODs from bacteria. In order to investigate the mechanism of product inhibition and whether it is a feature common to eukaryotic MnSODs, we purified MnSOD from Saccharomyces cerevisiae (ScMnSOD). It was a tetramer with 0.6 equiv of Mn per monomer. The catalytic activity of ScMnSOD was investigated by pulse radiolysis and compared with human and two bacterial (Escherichia coli and Deinococcus radiodurans) MnSODs. To our surprise, ScMnSOD most efficiently facilitates removal of high concentrations of O 2 - among these MnSODs. The gating value k 2/ k 3 that characterizes the level of product inhibition scales as ScMnSOD > D. radiodurans MnSOD > E. coli MnSOD > human MnSOD. While most MnSODs rest as the oxidized form, ScMnSOD was isolated in the Mn 2+ oxidation state as revealed by its optical and electron paramagnetic resonance spectra. This finding poses the possibility of elucidating the origin of product inhibition by comparing human MnSOD with ScMnSOD. © 2010 American Chemical Society.
DOI
10.1021/ja104179r
Appears in Collections:
일반대학원 > 바이오융합과학과 > Journal papers
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