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Single molecules

A protein in the spotlight

Nature Nanotechnology volume 7, pages 616–617 (2012)Cite this article

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The photocurrent of a single photosynthetic protein can be measured by using a scanning probe tip as both an electrode and a localized light source.

Over the past decade, techniques capable of studying single proteins have provided valuable insights into biological processes that would have been inaccessible with ensemble studies1. These techniques often rely on fluorescence and have, for example, revealed temporal fluctuations in the catalytic activity of enzymes2. In the case of redox enzymes, it may also be possible to extract mechanistic and kinetic information if the current related to the electron transfer could be measured in a single redox protein3. However, the minute catalytic current of an individual protein is typically well below the detection limit of state-of-the-art instrumentation, and even with highly active hydrogenases and the use of nanoelectrodes to minimize the background current, an ensemble of tens of enzymes has been required to reach a detectable catalytic current4. Writing in Nature Nanotechnology, Joachim Reichert, Itai Carmeli and colleagues have now shown that the photocurrent of a single redox protein, photosystem I (PS I), can be measured using a scanning tunnelling microscope (STM) set-up5.

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Figure 1: Measuring the photocurrent of a single PS I protein.

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Authors and Affiliations

  1. Nicolas Plumeré is at the Center for Electrochemical Sciences, Faculty for Chemistry and Biochemistry, Ruhr University Bochum, 44780 Bochum, Germany,

    Nicolas Plumeré

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  1. Nicolas Plumeré
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Correspondence to Nicolas Plumeré.

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Plumeré, N. A protein in the spotlight. Nature Nanotech 7, 616–617 (2012). https://doi.org/10.1038/nnano.2012.175

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  • DOI: https://doi.org/10.1038/nnano.2012.175

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