Published online by Cambridge University Press: 21 February 2011
Absorption spectra of Cytochrome c Peroxidase (CcP) in phosphate buffer atpH 6.5 were recorded from 700 to 250 nm. The CcP solution was thenencapsulated in sol-gel derived glass. The absorption spectra of CcP inxerogels were compared to those in buffer solutions. An increase inabsorptivity at the Soret maximum, a decrease between 360 and 380 nm, and aspectral shift of the charge-transfer band from 645 to 620 nm was observedfor CcP in gel matrix as compared to those in solution. Those spectralobservations indicate a change in the coordination of the iron porphyrinring 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 reactor to complex with the encapsulated CcP in sol-gel glass. The results showthat H2O2 and S2O42- lead to a change of oxidation state from Fe(III) to Fe(IV) andto Fe(II), respectively. Moreover, F- results in an enhancementof high-spin CcP, and N3- promotes a spin state change to alow-spin CcP. For CcP in xerogels, the chemical changes caused by inhibitorswere found to be reversible when washed with deionized water. The possibleapplications of CcP immobilized xerogels in chemical and biochemical sensortechnologies are discussed.