Electron transfer reactions are at the heart of biological energy production. For this reason, the importance of protein structure for defining the reduction potential and rate of electron transfer for metal co-factors has been a subject of study for many years. The advent of strategies to design, from scratch, metalloproteins capable of electron transfer reactions allows investigators to assess the importance of secondary structure for achieving desired redox centers. In this report, we will explore whether flexible loops or β-sheet structure are essential to obtain well-defined mononuclear centers such as found in Rubredoxin or Cupredoxins. It will be shown that FeS<sub>4</sub> electron transfer sites can be transferred into α-helical bundles in a manner that matches reduction potentials, spectroscopy and metal structure of native proteins. Obtaining mononuclear Cu environments with a bound thiolate within the core of helical bundles can also be accomplished, although the properties of the metal differ somewhat from some related native centers.

Metalloprotein design: Examination of mononuclear redox centers

253rd National Meeting (2017)

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