ScienceDaily (Nov. 5, 2009) — New insight into how nature handles some fundamental processes is guiding researchers in the design of tailor-made proteins for applications such as artificial photosynthetic centers, long-range electron transfers, and fuel-cell catalysts for energy conversion.
From rusting iron to forest fires to the beating of a human heart, oxidation-reduction reactions, which transfer electrons from one atom to another, are at the heart of many chemical and biological processes. Each process requires a particular redox potential, just as different electronic devices can require their own special battery.
How nature fine-tunes these potentials over a broad range with little change to the protein's electron-transfer properties or efficiency has largely remained a mystery.
Now, a team led by University of Illinois chemistry professor Yi Lu has unearthed nature's secret, and has utilized it to their advantage. The researchers describe their work in a paper to appear in the Nov. 5 issue of the journal Nature. "We show that two important interactions, hydrophobicity (water repelling) and hydrogen bonding, are capable of fine-tuning the reduction potential of a particular class of copper-containing proteins called cupredoxins," Lu said. "We extended the range both above and below what had previously been found in nature."
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http://www.sciencedaily.com/releases/2009/11/091104132702.htm