Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein design.

ABSTRACT: Nature has evolved diverse electron transport proteins and multiprotein assemblies essential to the generation and transduction of biological energy. However, substantially modifying or adapting these proteins for user-defined applications or to gain fundamental mechanistic insight can be hindered by their inherent complexity. De novo protein design offers an attractive route to stripping away this confounding complexity, enabling us to probe the fundamental workings of these bioenergetic proteins and systems, while providing robust, modular platforms for constructing completely artificial electron-conducting circuitry. Here, we use a set of de novo designed mono-heme and di-heme soluble and membrane proteins to delineate the contributions of electrostatic micro-environments and dielectric

SUBMITTER: Hardy BJ 

PROVIDER: S-EPMC11232281 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature