Rationally tuning the reduction potential of a single cupredoxin beyond the natural range.

摘要: Redox processes are at the heart of numerous functions in chemistry and biology, from long-range electron transfer photosynthesis respiration to catalysis industrial fuel cell research. These accomplished nature by only a limited number redox-active agents. A long-standing issue these fields is how redox potentials fine-tuned over broad range with little change site or electron-transfer properties. Resolving this will not advance our fundamental understanding roles long-range, non-covalent interactions processes, but also allow for design proteins having tailor-made applications such as artificial photosynthetic centres catalysts energy conversion. Here we show that two important secondary coordination sphere interactions, hydrophobicity hydrogen-bonding, capable tuning reduction potential cupredoxin azurin 700 mV range, surpassing highest lowest reported any mononuclear cupredoxin, without perturbing metal binding beyond what typical family proteins. We demonstrate effects individual structural features additive now predictable across full potentials.