Proteins are large, complex molecules, and their interactions within even the simplest of microorganisms are a complex and intriguing process, requiring a mechanistic understanding at the single molecule level that often defies the capabilities of current science and technology. Gaining insight into proteins and their interactions is crucial to our understanding of the biological world, and could provide technological advancement in alternative energy, drug discovery, and a wealth of other areas. Here, we are interested in the study of structural effects on the electron transfer properties of redox proteins. In particular, we are focused on generating protein fusions between photosystem I (PSI) of Synechocystis sp. PCC 6803 and the membrane-bound hydrogenase (MBH) of Ralstonia eutropha H16, a unique in vitro complex capable of harnessing solar energy for the production of molecular hydrogen (H2). We present our study of the detergent-solubilized solution structure of PSI using small-angle neutron scattering (SANS) experiments and all-atom molecular dynamics (AAMD) simulations, and discuss how this method is being applied to study PSI-MBH protein fusions. By utilizing a combination of computational modeling and experimental characterization of these fusion complexes, we hope to provide a novel approach for probing the structure-function relationship that governs redox proteins. Figure 1. <img src='https://acs-archive-assets2.s3.amazonaws.com/240nm/uploads/33857_figure1.jpg' alt='' />

Characterizing the structure-function relationship that governs electron transport in redox proteins

247th National Meeting (2014)

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