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Last Updated: 3 years ago

Possible Interaction: Cysteine and Cupric Cation

supplement:

Cysteine

supplement:

Cupric Cation

Research Papers that Mention the Interaction

Ascorbate and cysteine , which will reduce Cu2+ but have little or no affinity for Cu+, also stimulated GSNO decomposition in the presence of Cu2+ , but did not inhibit it at higher concentrations.
Archives of biochemistry and biophysics  •  1996  |  View Paper
Furthermore, selectivity experiments show that Cu(II) is a much more potent inhibitor for Cys compared to other metal ions.
When Cys was preincubated with Cu(II) , the fluorescence of the probe was decreased due to the inhibition of Cys's reactivity by Cu(II).
Talanta  •  2016  |  View Paper
L-Cysteine (CYS, 25 microM-1 mM) inhibited Cu2+ -dependent, but facilitated Fe3+-dependent, oxidation of LDL in a dose-dependent manner.
Biochimica et biophysica acta  •  1997  |  View Paper
Fluorescence drops linearly as the concentration of Cu2+ is increased from 50 nM to 1.0 µM, … detection limit for Cu2+ is calculated as 15 nM. By virtue of the strong interaction between Cys … Cu2+ , the GO-GABA/Cu2+ complex can further … recognize Cys in a “switch-on” mode.
Microchimica Acta  •  2019  |  View Paper
L-cysteine only protected from Cu(II) , to a limited degree (Table 4).
Medicina  •  1994  |  View Paper
The activation by cysteine was enhanced by the addition of Fe2+, Ni2+ or Cu2+.
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine  •  1970  |  View Paper
In the in vitro PPO solution, the inhibitory effect of L-cysteine on PPO activity was related to the decrease in pH and the ability of chelating Cu2+.
Foods  •  2021  |  View Paper
According to the "off-on-off" fluorescence cycle of BNC generated by the alternate addition of Cu2+ and Cys , a reversible memorized device with "read-write-read-erase" behavior was constructed at the molecular level.
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy  •  2020  |  View Paper
Mechanism study revealed that the intercalated cysteine in the interlayer of LDH strongly accelerated the rate-determining conversion of Cu(II ) to Cu(I) by oxidation itself to cystine, thus enhanced the catalytic efficiency for H2O2 activation to produce •OH radicals.
Journal of colloid and interface science  •  2019  |  View Paper
Herein we report fluorinated macrocyclic copper complexes that display a 19F NMR/MRI turn-on response following reduction of the Cu(ii) complexes by cysteine.
Dalton transactions  •  2018  |  View Paper
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