Factors influencing the electron-transfer rates of redox proteins.
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Biomedical subjects
Publications and source records attributed to M J Eddowes.
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Redox proteins catalyse the reactions of a wide variety of otherwise intractable substrates, such as dinitrogen, alkanes, arenes, terpenes and steroids. Two major factors impede the utilization of these enzymes--the inefficient electron transfer between the enzyme and electrode, and the properties often, but not inevitably, associated with enzymes, such as instability, complexity, and expense. We have now shown that the former can be overcome and that proteins can be coupled, via electrodes, to a number of energy sources; the latter is the subject of much effort elsewhere. We demonstrated previously that certain redox proteins can be reduced very efficiently electrochemically (Fig. 1a). Light and hydrogen are the two other convenient energy sources that could be used for such reductions, and we now report the reduction of cytochrome c by these means.
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Models describing the binding of antigens to surface immobilised antibodies have been developed. These models are applied to the assessment of the likely analytical utility of direct immunochemical sensors employing immobilised antibody layers. Fundamental limitations to the device response arising from the equilibrium and kinetic characteristics of the binding reaction and from mass transport constraints imply that measurement over the micromolar to nanomolar concentration range may be practical.