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• W2032171922 endingPage "1152" @default.
• W2032171922 startingPage "1131" @default.
• W2032171922 abstract "Monolayers of molecules, which retain their function in the adsorbed state on solid surfaces, are important in materials science, analytical detection, and other technology approaching the nanoscale. Molecular monolayers, including layers of functional biological macromolecules, offer new insight in electronic properties and stochastic single-molecule features and can be probed by new methods which approach the single-molecule level. One of these is in situ scanning tunneling microscopy (STM) in which single-molecule electronic properties directly in aqueous solution are probed. In situ STM combined with physical electrochemistry, single-crystal electrodes, and spectroscopic methods is now a new dimension in interfacial bioelectrochemistry. We overview first some approaches to spectroscopic single-molecule imaging, including fluorescence spectroscopy, chemical reaction dynamics, atomic force microscopy, and electrochemical single-electron transfer. We then focus on in situ STM. In addition to high structural resolution, in situ STM offers a single-molecule spectroscopic perspective. This emerges most clearly when adsorbate molecules contain accessible redox levels, and the tunneling current decomposes into successive single-molecule interfacial electron transfer (ET) steps. Theories of electrochemical ET and in situ STM of redox molecules as well as specific cases are addressed. Two-step in situ STM represents different molecular mechanisms and even new ET phenomena, related to coherent many-electron transfer. A number of systems are noted to accord with these views. The discussion is concluded by attention to one of the still very few redox proteins addressed by in situ STM, the blue copper protein Pseudomonas aeruginosa azurin. Use of comprehensive electrochemical techniques has ascertained that well-defined protein monolayers in two opposite orientations can be formed and interfacial tunneling patterns disclosed. P. aeruginosa azurin emerges as by far the most convincing case where in situ STM of functional metalloproteins to single-molecule resolution has been achieved. This comprehensive approach holds promise for broader use of in situ STM as a single-molecule spectroscopy of metalloproteins and illuminates prerequisites and limitations of in situ STM of biological macromolecules." @default.
• W2032171922 created "2016-06-24" @default.
• W2032171922 creator A5006162153 @default.
• W2032171922 creator A5010430951 @default.
• W2032171922 creator A5014876576 @default.
• W2032171922 creator A5047222708 @default.
• W2032171922 creator A5052561133 @default.
• W2032171922 creator A5057669612 @default.
• W2032171922 creator A5065984968 @default.
• W2032171922 creator A5083245206 @default.
• W2032171922 date "2002-01-17" @default.
• W2032171922 modified "2023-10-16" @default.
• W2032171922 title "Electronic Properties of Functional Biomolecules at Metal/Aqueous Solution Interfaces" @default.
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