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Cytochrome cyclic voltammogram

FIG. 26 Cyclic voltammograms of 40 monolayers of Langmuir-Schaefer films of cytochrome P450SCC on indium-tin oxide glass plate (ITO) in 10 mM phosphate buffer at a scan rate of 20 mV/s between 0.4 and —0.4 V vs. Ag/AgCl. LS films on ITO worked as the working electrode, platinum as the counter, and Ag/AgCl as the reference electrode. Cholesterol dissolved in X-triton 100 was added 50 p.1 at a time (1) with cholesterol, (2) 50 p.1 of cholesterol, (3) 100 p.1 cholesterol, and (4) 150 p.1 of cholesterol. [Pg.173]

Figure 3.89 Cyclic voltammograms of 500 pm cytochrome c at a gold electrode modified by (a) 2-mercaptopyridine, (b> 2-mercaptosuccinic acid, 4,4 -dithiobis(butanoic acid), (d) 4-mercaploaniline. pH 7.0 phosphate buffer +0.1 M NaC104. Scan rale 50mVs . From Allen... Figure 3.89 Cyclic voltammograms of 500 pm cytochrome c at a gold electrode modified by (a) 2-mercaptopyridine, (b> 2-mercaptosuccinic acid, <c> 4,4 -dithiobis(butanoic acid), (d) 4-mercaploaniline. pH 7.0 phosphate buffer +0.1 M NaC104. Scan rale 50mVs . From Allen...
Figures 3.91(a) and (b) show cyclic voltammograms of the SERS electrode in aqueous solutions of the SSBipy and PySH. In the potential range —0.3 V to 0.3 V vs. SCE, which is the range of interest for the reversible reduction of cytochrome c, no notable faradaic currents were observed for either of these species. However, at potentials < —0.4 V SSBipy is reduced to PySH and the PySH so formed is re-oxidised to SSBipy at potentials >0.1 V. Similarly, PySH is oxidised to SSBipy at potentials >0.1 V and this product re-reduced at potentials < —0.4 V. Figures 3.91(a) and (b) show cyclic voltammograms of the SERS electrode in aqueous solutions of the SSBipy and PySH. In the potential range —0.3 V to 0.3 V vs. SCE, which is the range of interest for the reversible reduction of cytochrome c, no notable faradaic currents were observed for either of these species. However, at potentials < —0.4 V SSBipy is reduced to PySH and the PySH so formed is re-oxidised to SSBipy at potentials >0.1 V. Similarly, PySH is oxidised to SSBipy at potentials >0.1 V and this product re-reduced at potentials < —0.4 V.
Figure 3 shows the cyclic voltammograms of cytochrome c recorded in aqueous solution either when the protein is adsorbed (or immobilized) on the electrode (Sn02) surface (a), or when it diffuses to a gold electrode pretreated by adsorption of 4,4 -bipyridyl (b). [Pg.544]

Figure 3 Cyclic voltammograms recorded at different scan rates in aqueous solution (pH 7) of cytochrome c, under the following experimental conditions (a) protein adsorbed on the Sn02 electrode surface (b) Au electrode pretreated with bipyridyl protein in solution... Figure 3 Cyclic voltammograms recorded at different scan rates in aqueous solution (pH 7) of cytochrome c, under the following experimental conditions (a) protein adsorbed on the Sn02 electrode surface (b) Au electrode pretreated with bipyridyl protein in solution...
Figure 4 (a) Typical cyclic voltammogram of cytochrome c recorded at a gold electrode... [Pg.546]

Within the promoter there can be subtle structural differences that influence the polar interaction with the protein. For example, Figure 5 illustrates the cyclic voltammograms of cytochrome c obtained at a gold electrode modified with isomers of pyridine-carboxylaldehyde-thiosemi-carbazone (PATS). [Pg.546]

Figure 5 Cyclic voltammograms of cytochrome c recorded at gold electrodes modified with different isomers of PATS... Figure 5 Cyclic voltammograms of cytochrome c recorded at gold electrodes modified with different isomers of PATS...
Figure 7 Cyclic voltammograms of cytochrome c recorded at different types of pyrolitic graphite electrodes. Also shown are the relative ESCA spectral patterns which show the 0/C ratio in the different treated electrode material (a scale enlargement (x3) is shown for the Ojs peak)... Figure 7 Cyclic voltammograms of cytochrome c recorded at different types of pyrolitic graphite electrodes. Also shown are the relative ESCA spectral patterns which show the 0/C ratio in the different treated electrode material (a scale enlargement (x3) is shown for the Ojs peak)...
Figure 8 Cyclic voltammograms of cytochrome c recorded at an edge-oriented pyrolitic graphite electrode. In the absence (a) and in the presence (b) of [Cr(NH3)6]3 +... Figure 8 Cyclic voltammograms of cytochrome c recorded at an edge-oriented pyrolitic graphite electrode. In the absence (a) and in the presence (b) of [Cr(NH3)6]3 +...
Figure 10 Cyclic voltammograms at a modified gold electrode (see text) of (a) cytochrome c (b) cytochrome f. Aqueous solution buffered at pH 7.3... Figure 10 Cyclic voltammograms at a modified gold electrode (see text) of (a) cytochrome c (b) cytochrome f. Aqueous solution buffered at pH 7.3...
Figure 11 Cyclic voltammogram of cytochrome b5 recorded at a gold electrode pretreated with Cys-Lys-Cys. Aqueous solution at pH 7.0 (KCl 0.1 mol dm 3). Scan rate 0.005 Vs 1... Figure 11 Cyclic voltammogram of cytochrome b5 recorded at a gold electrode pretreated with Cys-Lys-Cys. Aqueous solution at pH 7.0 (KCl 0.1 mol dm 3). Scan rate 0.005 Vs 1...
Figure 13 Cyclic voltammograms recorded at a glassy carbon electrode in an aqueous solution (pH 7) of cytochrome c3. Scan rates 0.002, 0.004, 0.007 V s ... Figure 13 Cyclic voltammograms recorded at a glassy carbon electrode in an aqueous solution (pH 7) of cytochrome c3. Scan rates 0.002, 0.004, 0.007 V s ...
Cyclic voltammograms recorded in an aqueous solution of cytochrome c (pH 7.1) at gold electrodes modified by (a) 3-hydroxo-l-propanthiol (b) 11-hydroxo-l-undecanthiol. Scan rate 0.5 V s . T = 0°C... [Pg.554]

Figure 15 Cyclic voltammogram recorded in a aqueous solution (pH= 7) of a cytochrome P450cam-DMPC thin film at a basal plane pyrolitic graphite electrode. Scan rate 0.1 V s l... Figure 15 Cyclic voltammogram recorded in a aqueous solution (pH= 7) of a cytochrome P450cam-DMPC thin film at a basal plane pyrolitic graphite electrode. Scan rate 0.1 V s l...
Cytochrome a, 36 245 Cytochrome a, 36 245, 249 Cytochrome b 36 429 cyclic voltammogram, 36 354-355 mixtures, cyclic voltammogram, 36 356-357 optical absorption spectrum, 36 418, 420 Cytochrome bjjg, 36 234 Cytochrome b,s2, four-helix bundle arrangement, 46 444... [Pg.72]

Fig. 14.28. Cyclic voltammograms of 100 n/W horse heart cytochrome cat an Au(110) surface modified with 4,4 -PySSPy, 2,2 -PySSPy, and diphenyl disulfide (PhSSPh) in a 0.1 M phosphate buffer solution containing 0.1 M NaCI04 (pH 7) at 25 °C. Scan rate 50 mV/s. (Reprinted from I. Taniguchi, Probing Metalloproteins and Bioelec-trochemical Systems, Interfacial 6(4) 34-37, Fig. 3, 1997. Reproduced by permission of the Electrochemical Society, Inc.)... Fig. 14.28. Cyclic voltammograms of 100 n/W horse heart cytochrome cat an Au(110) surface modified with 4,4 -PySSPy, 2,2 -PySSPy, and diphenyl disulfide (PhSSPh) in a 0.1 M phosphate buffer solution containing 0.1 M NaCI04 (pH 7) at 25 °C. Scan rate 50 mV/s. (Reprinted from I. Taniguchi, Probing Metalloproteins and Bioelec-trochemical Systems, Interfacial 6(4) 34-37, Fig. 3, 1997. Reproduced by permission of the Electrochemical Society, Inc.)...
Figure 4. The electron-transfer process from an Au electrode to soluble heme proteins as mediated by a monolayer of microperoxidase-11. Cyclic voltammograms of a microperoxidase-11 monolayer-electrode in the absence (a) and presence of added hemoproteins (b) with hemoglobin, 6 X 10 M (c) with myoglobin, 2 x 10 M (d) with cytochrome c, 2 x 10 M. Measurements recorded in 0.1 M phosphate buffer, pH 7.0, under Ar potential scan rate, 5 mV s. ... Figure 4. The electron-transfer process from an Au electrode to soluble heme proteins as mediated by a monolayer of microperoxidase-11. Cyclic voltammograms of a microperoxidase-11 monolayer-electrode in the absence (a) and presence of added hemoproteins (b) with hemoglobin, 6 X 10 M (c) with myoglobin, 2 x 10 M (d) with cytochrome c, 2 x 10 M. Measurements recorded in 0.1 M phosphate buffer, pH 7.0, under Ar potential scan rate, 5 mV s. ...
Figure 21. (A) The assembly of an integrated nitrate sensor electrode by the cross-linking of a microperoxidase-11-nitrate reductase (cytochrome-dependent, EC 1.9.6.1) affinity complex on an Au electrode. (B) Cyclic voltammograms of the integrated MP-ll-NR monolayer-modified Au electrode (roughness factor ca. 15). (a) 0.1 M phosphate buffer, pH 7.0 (b) in the presence of KNO3, 20 mM. Potential scan rate, 5 mV s . Inset electrocatalytic cathodic currents [E = —0.6 V vs. SCE) transduced by the modified electrode at different concentrations of KNO3. Measurements were performed under argon. Figure 21. (A) The assembly of an integrated nitrate sensor electrode by the cross-linking of a microperoxidase-11-nitrate reductase (cytochrome-dependent, EC 1.9.6.1) affinity complex on an Au electrode. (B) Cyclic voltammograms of the integrated MP-ll-NR monolayer-modified Au electrode (roughness factor ca. 15). (a) 0.1 M phosphate buffer, pH 7.0 (b) in the presence of KNO3, 20 mM. Potential scan rate, 5 mV s . Inset electrocatalytic cathodic currents [E = —0.6 V vs. SCE) transduced by the modified electrode at different concentrations of KNO3. Measurements were performed under argon.
Fig. 1.1. (a) SPR angle shifts (A pi) showing the electrostatical adsorption of cytochrome-c on gold electrode surfaces modified with a 3-mercaptopropionic acid SAM (I) after addition of cytochrome-c to a final concentration of ca. 2.5 x 10 M in 5 mM Na-phosphate pH 7.0 (full fine) or in 5 mM Na-phosphate, 100 mM KCl pH 7.0 (dotted line) (11) after rinsing the surface with clean buffer solution, (b) Cyclic voltammograms of a monolayer of cytochrome-c adsorbed on a gold electrode modified with a 3-mercaptopropionic add SAM recorded in 5 mM Na-phosphate, pH 7.0, at 50, 100 and 200 mV s. Reproduced fix)m [214] with permission. [Pg.35]

Fig. 2. Cyclic voltammograms of horse heart cytochrome c at pyrolytic graphite electrodes 0,15 mM protein in 5 mM Tricine/100 mM NaCl, pH 8.0. Scan rate 20 mV sec. ... Fig. 2. Cyclic voltammograms of horse heart cytochrome c at pyrolytic graphite electrodes 0,15 mM protein in 5 mM Tricine/100 mM NaCl, pH 8.0. Scan rate 20 mV sec. ...
Fig. 3. Cyclic voltammograms of the yeast cytochrome c mutant, He 13 (180 nM), at a 4,4 -bipyridyl disulfide-modified gold electrode 20 mV sec , 10 toM HEPES/100 mM KCl, pH 7.4. (a) Initial scan (b) final scan. Fig. 3. Cyclic voltammograms of the yeast cytochrome c mutant, He 13 (180 nM), at a 4,4 -bipyridyl disulfide-modified gold electrode 20 mV sec , 10 toM HEPES/100 mM KCl, pH 7.4. (a) Initial scan (b) final scan.
Fig 5. Cyclic voltammograms of (A) cytochrome c alone (95 ixM), (B) cytochrome 65 alone (95 nM), (C) cytochrome c with cytochrome 65 (95 ijlM each), (D) Zn(II)-cyto-chrome e alone (75 ixM), and (E) cytochrome with Zn(II)-cytochrome c (75 ijlM each) at an edge-plane graphite electrode 1 mM HEPES/20 raM KCl, pH 7.0. Scan rate 10 mV... [Pg.355]

Fig. 7, Cyclic voltammogram of 1 1 cross-linked cytochrome c/plastocyanin (—) and a 1 1 mixture of free proteins (—) at an edge-plane graphite electrode 50 iaM protein in 20 mM cacodylate, pH 7.0. Scan rate 10 mV sec L... Fig. 7, Cyclic voltammogram of 1 1 cross-linked cytochrome c/plastocyanin (—) and a 1 1 mixture of free proteins (—) at an edge-plane graphite electrode 50 iaM protein in 20 mM cacodylate, pH 7.0. Scan rate 10 mV sec L...
Camphor sulfonic acid CV cyclic voltammogram CYP2D6 — cytochrome P450-2D6 DBSA dodecyl benzenesulfonic acid EAQ — Eastman AQ polymersTM FTIR — Fourier Transform infrared spectroscopy HRP — Horseradish peroxidase NMP N-methylpyrollidone PTM particle track-etched membrane PANIs... [Pg.40]


See other pages where Cytochrome cyclic voltammogram is mentioned: [Pg.170]    [Pg.171]    [Pg.228]    [Pg.364]    [Pg.374]    [Pg.72]    [Pg.375]    [Pg.379]    [Pg.36]    [Pg.286]    [Pg.344]    [Pg.347]    [Pg.352]    [Pg.357]    [Pg.361]    [Pg.173]   
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