Scanning Probe Studies of Metalloprotein

应用文章

Redox reactions are of central importance in sustaining all life and are mediated in nature by highly specific “interaction surfaces.” We are interested in the analysis and control of biological redox proteins/enzymes with electrode surfaces. Azurins are well-characterized blue copper proteins that function as “electron shuttles” in certain bacteria. Of the many enzymes known to catalyze redox reactions involving molecular oxygen, the cytochrome P450 monooxygenases are presently attracting much attention. These b-haem containing oxidases, which are widely distributed in nature, are able to catalyze the controlled activation of dioxygen and play a role in the biosynthesis of steroids, drug metabolism, the bioactivation of polycyclic aromatic hydrocarbons (PAHs) to carcinogens, and detoxification. Presently, much interest in P450 enzymes is associated with attempts to attain reproducible voltammetric responses (1). If these responses can be achieved with the enzyme immobilized in an active form, then one can postulate the generation of derived biosensing systems targeting specific compounds.

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