Fine-tuning protein potential

Tailor-made proteins for applications such as artificial photosynthetic centers, long-range electron transfers, and fuel-cell catalysts for energy conversion might be possible thanks to advances in natural redox processes. Yi Lu of the University of Illinois and colleagues have shown that hydrophobic interactions and hydrogen bonding can be exploited to fine-tune the redox potential of copper-containing cupredoxin proteins. "We have now extended the range both above and below what had previously been found in nature," Lu says.