Biomolecular Films (Surfactant Science Series) by James F. Rusling

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By James F. Rusling

Surveying detailed and smooth biomolecular movie methodologies and investigative ideas, this article examines motion pictures of biomolecules which could supply sturdy surfaces for catalyzing enzyme reactions, serve in biosensors and as biorecognition parts, mediate nanoparticle formation, and supply a foundation for basic experiences and purposes in biomedicine and biomedical units. The authors speak about designing sensible biomolecular motion pictures on electrodes, biomimetic membranes on steel helps, peptide and protein-based biomolecular assemblies, floor plasmon resonance spectroscopy, and biosensors.

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Conversion of styrene to styrene oxide [68À70]. Catalytic amperometric and voltammetric responses of peroxidase ¢lms to hydrogen peroxide are likely to be related to a pathway similar to Scheme 4 [71]. Stable ¢lms of DMPC containing M. tuberculosis catalaseperoxidase (KatG), several peroxidases, myoglobin, or catalase gave reversible FeIII=FeII voltammetry on pyrolytic graphite electrodes, and catalytic Designing Functional Biomolecular Films 23 FIG. 10 Idealized voltammograms computed from theory for a rotating disk electrode: (a) reversible thin enzyme film; (b) catalytic current for a thin enzyme film and substrate (reactant) in solution featuring a steady-state current beyond the protein reduction potential.

26 Rusling and Zhang Monolayer ¢lm voltammetry has been used for seminal studies of electron transfer properties, coupled chemical processes, and enzyme catalysis for a variety of proteins. For details,we refer the reader to recent reviews [66,78], and to the original literature cited therein. The method has been used for many kinetic, mechanistic, and H=D isotope studies of catalysis by native and mutant enzymes [66,85À87]. The most recent studies of thin protein monolayers by voltammetry demonstrate increasingly sophisticated mechanistic resolving power.

In the absence of reactive substrate in solution, rotating the electrode has no e¡ect on the shape of a reversible thin protein ¢lm voltammogram because the electrochemistry is insensitive to mass transport external to the ¢lm. Addition of substrate to the solution provides catalytic steady-state voltammograms by RDV. The currentÀpotential curve now assumes a sigmoid shape (Fig. 10) with a steady-state plateau current. The Michaelis-Menton formulation of enzyme kinetics postulates an enzymeÀsubstrate (reactant) complex with dissociation constant KM and turnover rate constant kcat for the conversion of this enzymeÀsubstrate complex to product.

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