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Myoglobin voltammetry

PSS-SG composite film was tested for sorption of heme proteins hemoglobin (Hb) and myoglobin (Mb). The peroxidaze activity of adsorbed proteins were studied and evaluated by optical and voltammetric methods. Mb-PSS-SG film on PG electrode was shown to be perspective for detection of dissolved oxygen and hydrogen peroxide by voltammetry with linear calibration in the range 2-30 p.M, and detection limit -1.5 p.M. Obtained composite films can be modified by different types of biological active compounds which is important for the development of sensitive elements of biosensors. [Pg.306]

A variety of physical methods has been used to ascertain whether or not surface ruthenation alters the structure of a protein. UV-vis, CD, EPR, and resonance Raman spectroscopies have demonstrated that myoglobin [14, 18], cytochrome c [5, 16, 19, 21], and azurin [13] are not perturbed structurally by the attachment of a ruthenium complex to a surface histidine. The reduction potential of the metal redox center of a protein and its temperature dependence are indicators of protein structure as well. Cyclic voltammetry [5, 13], differential pulse polarography [14,21], and spectroelectrochemistry [12,14,22] are commonly used for the determination of the ruthenium and protein redox center potentials in modified proteins. [Pg.111]

The temperature dependence of the kinetics of myoglobin has been studied using cyclic voltammetry. These experiments were conducted over a range of temperatures (10-50 °C) to determine the change in reaction center entropy... [Pg.473]

Figure 6 Background-subtracted cyclic voltammetry of metmyoglobin (A) 86 J,M met-myoglobin, pH 7.0 (B) 67 mM metmyoglobin, pH 7.0, with excess cyanide to give [Mb(III)Hp] [CN-] of 1 300. Scan rates 20, 50, 100, 200 mV/s. Figure 6 Background-subtracted cyclic voltammetry of metmyoglobin (A) 86 J,M met-myoglobin, pH 7.0 (B) 67 mM metmyoglobin, pH 7.0, with excess cyanide to give [Mb(III)Hp] [CN-] of 1 300. Scan rates 20, 50, 100, 200 mV/s.
Our research group first danonstrated that layer-by-layer adsorption can provide ultrathin myoglobin and cyt P450 films featuring direct electron exchange with electrodes [81]. An undercoating of mercaptopropanesulfonate (MPS) on gold electrodes was necessary to faciUtate direct voltammetry of the... [Pg.214]

Yu et al. have covalently linked myoglobin and horseradish peroxidase to an aligned SWCNT electrode through the amide linkage. Quasi-reversible Ee +/Ee + voltammetry was observed for the iron heme enzymes, myoglobin, and horseradish peroxidase. The results demonstrated that the trees in the nanotube forest are potent current collectors that conduct electrons from the external circuit to the redox sites of the enzymes. [Pg.204]

Yu et al. showed that SWCNT forest electrodes could be used to observe direct reversible electrochemistry of proteins HRP and myoglobin, and Gooding et al. obtained reversible voltammetry for the heme-containing peptide microperoxidase MP-11 derived from cyt c. Yu et al. assembled oxidized SWCNTs 20-30 nm in length onto a composite bed of Nafion ionomer and precipitated Fe + hydroxides on ordinary pyrolytic graphite (Figure 13.7). Myoglobin or HRP was covalently attached to the ends... [Pg.481]


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Myoglobin

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