Hostname: page-component-78c5997874-4rdpn Total loading time: 0 Render date: 2024-11-10T08:58:16.466Z Has data issue: false hasContentIssue false

Nitric Oxide Sensors obtained through the entrapment of iron complexes in sol-gel matrix

Published online by Cambridge University Press:  01 February 2011

Juliana C. Biazzotto
Affiliation:
Departamento de Física e Matemática-FFCLRP-USP, Av. Bandeirantes 3900, 14040-901
João F. Borin
Affiliation:
Departamento de Física e Matemática-FFCLRP-USP, Av. Bandeirantes 3900, 14040-901
Roberto Mendonça Faria
Affiliation:
Brazil-Instituto de Física de São Carlos-USP, C.P. 369, 13560-970 São Carlos, Brazil
Carlos F.O Graeff
Affiliation:
Departamento de Física e Matemática-FFCLRP-USP, Av. Bandeirantes 3900, 14040-901
Ribeirão Preto
Affiliation:
Departamento de Física e Matemática-FFCLRP-USP, Av. Bandeirantes 3900, 14040-901
Get access

Abstract

Iron(III)-diethyldithiocarbamate (Fe3DETC) or iron(III)-tetra-pentafluorophenyl porphyrin (FeTFPP) was entrapped within a silica matrix by the sol-gel process. The obtained sol-gel materials SGFeDETC and SGFeTFPP were investigated as sensors for nitric oxide (NO). UV/Vis spectra of the SGFeTFPP present a Soret band at 410 nm similar to that found in the solution. The binding of gaseous NO resulted in a red shift in the Soret absorption band (410 to 419 nm) of the FeTFPP in the matrix unlike FeTFPP:NO in solution. In the case of SGFeDETC, after addition of sodium dithionite solution and bubbling NO we have good evidence that the complex is formed. The EPR spectrum of the SGFeDETC:NO in solid form exhibited a signal similar to that found in a solution of FeDETC:NO at 77K. The UV/Vis spectrum of SGFeDETC:NO shows a band at 367 nm also found in FeDETC:NO solutions. It is observed that the FeDETC:NO is more stable entrapped in the sol-gel than in aqueous solution. In the former the EPR signal decreases by a factor of 4 after one week, in the latter in 2 days the EPR signal cannot be observed anymore.

Type
Research Article
Copyright
Copyright © Materials Research Society 2002

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Garthwaite, J. and Boulton, C.L. Annu. Rev. Physiol. 57, 683 (1995)Google Scholar
2. Hibbs, J.B. Jr, Taintor, R.R. and Vavrin, Z. Science 235, 473 (1987)Google Scholar
3. Kotake, Y. Methods Enzymol. 268, 222 (1996)Google Scholar
4. Trévin, S., Bedioui, F. and Devynck, J. J. Electroanal. Chem. 408, 261 (1996)Google Scholar
5. Blyth, D.J. Aylott, J.W. Moir, J.W.B. Richardson, D.J. and Russell, D.A. Analyst 124, 129 (1999)Google Scholar
6. Corriu, R.J.P. and Leclercq, D. Angew. Chem. Int. Ed. Ingl. 35, 1420 (1996)Google Scholar
7. Vanin, A.F. Liu, X. Samouilov, A. Stukan, R.A. and Zweier, J.L. Biochim. Biophys. Acta 1474, 365 (2000)Google Scholar
8. Maruszewski, J. Mol. Struct. 479, 53 (1999)Google Scholar
9. Vanin, A.F. Biochemistry 60, 441 (1995)Google Scholar