Assembling Paramagnetic Ceruloplasmin at Electrode Surfaces Covered with Ferromagnetic Nanoparticles. Scanning Electrochemical Microscopy in the Presence of a Magnetic Field
Source abstract
Abstract
Adsorption of ceruloplasmin (Cp) at a gold electrode modified with ferromagnetic iron nanoparticles encapsulated in carbon (Fe@C Nps) leads to a successful immobilization of the enzyme in its electroactive form. The proper placement of Cp at the electrode surface on top of the nanocapsules containing an iron core allowed a preorientation of the enzyme, hence allowing direct electron transfer between the electrode and the enzyme. Laser ablation coupled with inductively coupled plasma mass spectrometry indicated that Cp was predominantly located at the paramagnetic nanoparticles. Scanning electrochemical microscopy measurements in the sample-generation/tip-collection mode proved that Cp was ferrooxidative inactive if it was immobilized on the bare gold surface and reached the highest activity if it was adsorbed on Fe@C Nps in the presence of a magnetic field.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Electrochemical Analysis and Applications · Trace Elements in Health · Electrochemical sensors and biosensors
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Faculty of Chemistry, University of Warsaw, ul. Pasteura 1, PL-02-093 Warsaw, Poland
Analytical Chemistry-Center for Electrochemical Sciences (CES), Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780 Bochum, Germany
Biological and Chemical Research Centre, Faculty of Chemistry, University of Warsaw, ul. Zwirki i Wigury 101, PL-02-093 Warsaw, Poland
Funding
Deutsche Forschungsgemeinschaft · Narodowe Centrum Nauki
References (51)
Show source-provided references
1. 10.1111/j.1753-4887.2010.00271.x10.1111/j.1753-4887.2010.00271.x ↗
2. Osaki S. · J. Biol. Chem. · 1996 · 241 · 274610.1016/S0021-9258(18)96527-0 ↗
3. 10.1038/jes.2008.210.1038/jes.2008.2 ↗
4. 10.1177/00045632780150017010.1177/000456327801500170 ↗
5. 10.1002/ana.41032070510.1002/ana.410320705 ↗
6. Patel B. N. · J. Neurosci. · 2002 · 22 · 657810.1523/JNEUROSCI.22-15-06578.2002 ↗
7. 10.4067/S0716-9760200600010000710.4067/S0716-97602006000100007 ↗
8. Osaki S. · J. Biol. Chem. · 1966 · 241 · 505310.1016/S0021-9258(18)99669-9 ↗
9. Osaki S. · J. Biol. Chem. · 1967 · 242 · 265310.1016/S0021-9258(18)99620-1 ↗
10. Huber T. · J. Biol. Chem. · 1970 · 245 · 397310.1016/S0021-9258(18)62943-6 ↗
11. 10.1111/j.1432-1033.1971.tb01523.x10.1111/j.1432-1033.1971.tb01523.x ↗
12. 10.1007/BF0278912910.1007/BF02789129 ↗
13. 10.1016/0014-5793(83)80432-310.1016/0014-5793(83)80432-3 ↗
14. Frieden E. · Adv. Enzymol. Ramb. · 1976 · 44 · 187
15. Zaitsev V. · Fold. Des. · 1996 · 1 · S7110.1016/S1359-0278(96)00036-3 ↗
16. 10.1016/j.bioelechem.2009.05.01210.1016/j.bioelechem.2009.05.012 ↗
17. 10.1021/cr950046o10.1021/cr950046o ↗
18. 10.1021/ja002339r10.1021/ja002339r ↗
19. 10.1016/j.jcis.2007.06.05910.1016/j.jcis.2007.06.059 ↗
20. 10.1021/ar00173a00210.1021/ar00173a002 ↗
21. 10.1016/0302-4598(86)85028-010.1016/0302-4598(86)85028-0 ↗
22. 10.1016/0302-4598(91)87023-A10.1016/0302-4598(91)87023-A ↗
23. 10.1016/0302-4598(96)01919-810.1016/0302-4598(96)01919-8 ↗
24. 10.1016/j.bios.2004.10.00310.1016/j.bios.2004.10.003 ↗
25. 10.1002/1521-4109(200105)13:8/9<669::AID-ELAN669>3.0.CO;2-S10.1002/1521-4109(200105)13:8/9<669::AID-ELAN669>3.0.CO;2-S ↗
26. 10.1007/s00216010079510.1007/s002160100795 ↗
27. 10.1016/j.bios.2006.07.03910.1016/j.bios.2006.07.039 ↗
28. 10.1016/S0956-5663(96)00056-510.1016/S0956-5663(96)00056-5 ↗
29. 10.1016/S0013-4686(97)00158-810.1016/S0013-4686(97)00158-8 ↗
30. 10.1246/cl.1999.97510.1246/cl.1999.975 ↗
31. 10.1021/ac990310410.1021/ac9903104 ↗
32. 10.1016/0003-2697(73)90374-610.1016/0003-2697(73)90374-6 ↗
33. 10.1016/j.materresbull.2011.08.04710.1016/j.materresbull.2011.08.047 ↗
34. 10.1039/c1ja10137d10.1039/c1ja10137d ↗
35. 10.1021/la00075a02410.1021/la00075a024 ↗
36. 10.1016/j.snb.2005.03.02910.1016/j.snb.2005.03.029 ↗
37. 10.1016/j.carbon.2008.07.01110.1016/j.carbon.2008.07.011 ↗
38. 10.1016/j.bios.2010.10.04610.1016/j.bios.2010.10.046 ↗
39. Lasia, A.InModern Aspects of Electrochemistry;Schlesinger, M., Ed.Springer:New York, 2009; pp67–138.
40. 10.1021/ac201794m10.1021/ac201794m ↗
41. 10.1111/j.1432-1033.1992.tb17464.x10.1111/j.1432-1033.1992.tb17464.x ↗
42. 10.1248/bpb.23.140610.1248/bpb.23.1406 ↗
43. 10.1016/j.bios.2014.09.07910.1016/j.bios.2014.09.079 ↗
44. 10.1016/0005-2795(73)90112-810.1016/0005-2795(73)90112-8 ↗
45. 10.1021/bi980434v10.1021/bi980434v ↗
46. Calabrese, L.; Musci, G.InMuli-copper oxidases;Messerschmidt, A., Ed.World Scientific:London, 1997; pp307–354.10.1142/9789812830081_0011 ↗
47. Guo L. · Adv. Inorg. Chem. · 1991 · 36 · 34110.1016/S0898-8838(08)60043-4 ↗
48. 10.1042/BJ2004101510.1042/BJ20041015 ↗
49. 10.1016/j.elecom.2006.03.00810.1016/j.elecom.2006.03.008 ↗
50. 10.1016/j.bbabio.2008.06.01010.1016/j.bbabio.2008.06.010 ↗
51. 10.1021/la402432q10.1021/la402432q ↗