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Evidence of Hexa-Coordination CcP Immobilized in Sol-Gel Glass

Published online by Cambridge University Press:  21 February 2011

Les B. Meuret
Affiliation:
Department of Chemistry, Northern Illinois University, DeKalb, IL 60115-2862
C. M. Catuara
Affiliation:
Department of Chemistry, Northern Illinois University, DeKalb, IL 60115-2862
A. M. Mahloudji
Affiliation:
Department of Chemistry, Northern Illinois University, DeKalb, IL 60115-2862
C. T. Lin
Affiliation:
Department of Chemistry, Northern Illinois University, DeKalb, IL 60115-2862
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Abstract

Absorption spectra of Cytochrome c Peroxidase (CcP) in phosphate buffer at pH 6.5 were recorded from 700 to 250 nm. The CcP solution was then encapsulated in sol-gel derived glass. The absorption spectra of CcP in xerogels were compared to those in buffer solutions. An increase in absorptivity at the Soret maximum, a decrease between 360 and 380 nm, and a spectral shift of the charge-transfer band from 645 to 620 nm was observed for CcP in gel matrix as compared to those in solution. Those spectral observations indicate a change in the coordination of the iron porphyrin ring in CcP from penta-coordinated in solutions to hexa-coordinated in gels. The oxidant H2O2, reductant Na2S2O4, and inhibitors NaF and KN3 were allowed to diffuse through the porous glass, to react or to complex with the encapsulated CcP in sol-gel glass. The results show that H2O2 and S2O42- lead to a change of oxidation state from Fe(III) to Fe(IV) and to Fe(II), respectively. Moreover, F- results in an enhancement of high-spin CcP, and N3- promotes a spin state change to a low-spin CcP. For CcP in xerogels, the chemical changes caused by inhibitors were found to be reversible when washed with deionized water. The possible applications of CcP immobilized xerogels in chemical and biochemical sensor technologies are discussed.

Type
Research Article
Copyright
Copyright © Materials Research Society 1998

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References

REFERENCES

1 Yonetani, T., in The Enzymes, edited by Boyer, P. D. (Academic Press, 13, New York, NY, 1976) pp. 345361.Google Scholar
2 Poulos, T. L. and Kraut, J., J. Biol. Chem. 255, 8199(1980).Google Scholar
3 Barb, W. G., Baxendale, J. H., George, P. and Hargrave, K. R., Trans. Faraday Soc. 47, 591(1951).Google Scholar
4 Weiss, C., J. Mol. Spectrosc. 44, 37(1972).Google Scholar
5 Day, P., Scregg, C. and Williams, R. J. P., Biopolymers Symposia, 1, 271(1964).Google Scholar
6 Hewson, W. D. and Hager, L. P., in The Porphyrin. edited by Dolphin, D. (Academic Press, 7, New York, NY, 1979) pp. 295332.Google Scholar
7 Yonetani, T., Schleyer, H. and Ehrenberg, A., J. Biol. Chem. 241, 3240(1966).Google Scholar
8 Griffith, J. S., Proc. Roy. Soc. (London), Ser. A, 235, 23(1956).Google Scholar
9 Yamanaka, S. A., Nishida, F., Ellerby, L. M., Nishida, C. R., Dunn, B., Valentine, J. S. and Zink, J. I., Chem. Mater. 4, 495(1992).Google Scholar
10 Braun, S., Rappoport, S., Zusman, R., Avnir, D. and Ottolenghi, M., Mater. Lett. 10, 1(1990).Google Scholar
11 Vitello, L. B., Huang, M. and Erman, J. E., Biochemistry, 29,4283(1990).Google Scholar
12 Yonetani, T., Wilson, D. F. and Seamonds, B., J. Biol. Chem. 241, 5347(1966).Google Scholar