2016
DOI: 10.1039/c6mb00458j
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S95C substitution in CuZn-SOD of Ipomoea carnea: impact on the structure, function and stability

Abstract: Superoxide dismutase (SOD) in general is a unique homo-dimeric enzyme that can scavenge toxic superoxide radicals by dismutation reaction. In IcSOD (Ipomoea carnea SOD), the presence of cysteine (Cys) plays an essential role in protein behaviour. This study analysed the role of Cys in modulating the stability and kinetic properties of IcSOD. To investigate the significance of the dimeric structure in modulating the structure/function relationship of CuZn-SODs, we have substituted a conserved serine by cysteine… Show more

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Cited by 12 publications
(4 citation statements)
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“…Cu, Zn-SOD mostly exists in homo-dimeric form with non-covalently attached Cu and Zn ions in each subunit 5 . While the zinc ion was found to be responsible for stabilizing the SOD dimer, the copper ion, via an alternate oxidation-reduction mechanism, helps this enzyme to catalyze a two-step superoxide dismutation reaction 6 . Certain Cu, Zn-SODs were also found to exhibit unaltered catalytic activity even in the presence of ionic detergents, chaotropic agents, extreme pH, and high temperature 7 9 .…”
Section: Introductionmentioning
confidence: 99%
“…Cu, Zn-SOD mostly exists in homo-dimeric form with non-covalently attached Cu and Zn ions in each subunit 5 . While the zinc ion was found to be responsible for stabilizing the SOD dimer, the copper ion, via an alternate oxidation-reduction mechanism, helps this enzyme to catalyze a two-step superoxide dismutation reaction 6 . Certain Cu, Zn-SODs were also found to exhibit unaltered catalytic activity even in the presence of ionic detergents, chaotropic agents, extreme pH, and high temperature 7 9 .…”
Section: Introductionmentioning
confidence: 99%
“…Hence, research on and developments of materials that are able to catalyze the production of ROS have attracted more and more attention from researchers and clinicians [3][4][5]. Metal ions, such as copper, iron, and manganese, are considered strong catalytic centers for the composition of reactive proteins in viable organisms that can produce ROS efficiently [6][7][8]. Recently, the synthesis of a series of ROS-catalyzing artificial enzymes has been achieved [9][10][11].…”
Section: Introductionmentioning
confidence: 99%
“…Hence, the development of compounds that can catalyze the production of ROS has attracted more and more attention [ 3 , 4 , 5 ]. Paired species, such as transition metal ions, are considered strong catalytic centers for constructing the reactive proteins in viable organisms, for example, hemoglobin (Hb), myoglobin (Mb), and superoxide dismutase (SOD), all of which can efficiently produce ROS [ 6 , 7 , 8 ]. In recent years, the synthesis of a range of artificial oxidase enzymes has been achieved [ 9 , 10 , 11 ].…”
Section: Introductionmentioning
confidence: 99%