A NITRITE BIOSENSOR BASED ON A MALTOSE-BINDING PROTEIN NITRITE REDUCTASE FUSION IMMOBILIZED ON AN ELECTROPOLYMERIZED FILM OF A PYRROLE DERIVED BIPYRIDINIUM
Q. Wu et al., A NITRITE BIOSENSOR BASED ON A MALTOSE-BINDING PROTEIN NITRITE REDUCTASE FUSION IMMOBILIZED ON AN ELECTROPOLYMERIZED FILM OF A PYRROLE DERIVED BIPYRIDINIUM, Analytical chemistry, 69(23), 1997, pp. 4856-4863
The preparation and electrochemical characterization of glassy carbon
electrodes (GCEs) modified with electropolymerized films of the cation
N-(3-pyrrol-1-yl-propyl)-4,4'-bipyridine (PPB) are described. The beh
avior of a new biosensor, which exhibits a high catalytic activity for
nitrite reduction and which consists of a maltose binding protein nit
rite reductase fusion (MBP-Nir) immobilized on an electropolymerized f
ilm of PPB as an electrocatalyst, is also described, The insoluble per
chlorate salt of the poly-(benzylviologen) dication was used to immobi
lize MBP-Nir onto an electrode previously modified with an electropoly
merized film of PPB, The electropolymerized film of PPB on the GCE is
redox active and exhibits special electron-transfer properties toward
the MBP-Nir layer but not toward Nit (Nir without MBP fusion attached)
, suggesting an intimate interaction between the PPB film and the MBP-
Nir layer. The kinetics of the catalytic reaction between the biosenso
r and nitrite anion were characterized using cyclic voltammetry and ro
tated disk electrode techniques, and a value of (4.6 +/- 0.5) x 10(3)
M-1 s(-1) was obtained for the rate constant.