journal article·2015-07-28

Assembling Paramagnetic Ceruloplasmin at Electrode Surfaces Covered with Ferromagnetic Nanoparticles. Scanning Electrochemical Microscopy in the Presence of a Magnetic Field

Edyta Matysiak, Alexander J. R. Botz, Jan Clausmeyer, Barbara Wagner, Wolfgang Schuhmann, Zbigniew Stojek, Anna M. Nowicka

Langmuir· Volume 31· Issue 29
Publisher page

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 ↗