Enzymatic activity and catalytic hydrogen evolution in reduced and oxidized urease at mercury surfaces

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F13%3A00422414" target="_blank" >RIV/68081707:_____/13:00422414 - isvavai.cz</a>
Alternative codes found
RIV/00209805:_____/13:#0000425
Result on the web
<a href="http://dx.doi.org/10.1016/j.aca.2013.06.014" target="_blank" >http://dx.doi.org/10.1016/j.aca.2013.06.014</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.aca.2013.06.014" target="_blank" >10.1016/j.aca.2013.06.014</a>

Result language
angličtina
Original language name
Enzymatic activity and catalytic hydrogen evolution in reduced and oxidized urease at mercury surfaces
Original language description
It was originally shown [10] that urease retains its enzymatic activity when adsorbed at bare mercury and solid amalgam surfaces. However the opinion later prevailed that, when adsorbed at bare metal electrodes, proteins are irreversibly denatured. Herewe confirm that urease is enzymatically active at a bare solid amalgam surface as found by Santhanam et al., and we show that this enzyme is equally active at a thiol-modified amalgam surface. We also show that it is the reduced form of urease, which isenzymatically active at Hg surfaces. Oxidation of the protein, resulting in formation of disulfide bonds, strongly decreases the enzyme activity. Using constant current chronopotentiometric stripping (CPS) we show that the exposure of surface-attached urease to negative potentials results in the protein unfolding.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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