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Comparison of two yeast mnsods: Mitochondrial saccharomyces cerevisiae versus cytosolic candida albicans

Title
Comparison of two yeast mnsods: Mitochondrial saccharomyces cerevisiae versus cytosolic candida albicans
Authors
Sheng Y.Stich T.A.Barnese K.Gralla E.B.Cascio D.Britt R.D.Cabelli D.E.Valentine J.S.
Ewha Authors
Joan S. Valentine
SCOPUS Author ID
Joan S. Valentinescopus
Issue Date
2011
Journal Title
Journal of the American Chemical Society
ISSN
0002-7863JCR Link
Citation
vol. 133, no. 51, pp. 20878 - 20889
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Human MnSOD is significantly more product-inhibited than bacterial MnSODs at high concentrations of superoxide (O 2 -). This behavior limits the amount of H 2O 2 produced at high [O 2 -]; its desirability can be explained by the multiple roles of H 2O 2 in mammalian cells, particularly its role in signaling. To investigate the mechanism of product inhibition in MnSOD, two yeast MnSODs, one from Saccharomyces cerevisiae mitochondria (ScMnSOD) and the other from Candida albicans cytosol (CaMnSODc), were isolated and characterized. ScMnSOD and CaMnSODc are similar in catalytic kinetics, spectroscopy, and redox chemistry, and they both rest predominantly in the reduced state (unlike most other MnSODs). At high [O 2 -], the dismutation efficiencies of the yeast MnSODs surpass those of human and bacterial MnSODs, due to very low level of product inhibition. Optical and parallel-mode electron paramagnetic resonance (EPR) spectra suggest the presence of two Mn 3+ species in yeast Mn 3+SODs, including the well-characterized 5-coordinate Mn 3+ species and a 6-coordinate L-Mn 3+ species with hydroxide as the putative sixth ligand (L). The first and second coordination spheres of ScMnSOD are more similar to bacterial than to human MnSOD. Gln154, an H-bond donor to the Mn-coordinated solvent molecule, is slightly further away from Mn in yeast MnSODs, which may result in their unusual resting state. Mechanistically, the high efficiency of yeast MnSODs could be ascribed to putative translocation of an outer-sphere solvent molecule, which could destabilize the inhibited complex and enhance proton transfer from protein to peroxide. Our studies on yeast MnSODs indicate the unique nature of human MnSOD in that it predominantly undergoes the inhibited pathway at high [O 2 -]. © 2011 American Chemical Society.
DOI
10.1021/ja2077476
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일반대학원 > 바이오융합과학과 > Journal papers
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