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Cytochrome c

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Intermolecular Electron Transfer Reactivity And Dynamics Of Cytochrome C – Nanoparticle Adducts, Adrienne M. Carver Sep 2009

Intermolecular Electron Transfer Reactivity And Dynamics Of Cytochrome C – Nanoparticle Adducts, Adrienne M. Carver

Open Access Dissertations

Interprotein electron transfer (ET) is crucial for natural energy conversion and a fundamental reaction in the pursuit of understanding the broader problem of proteinprotein interactions and reactivity. Simplifying the complicated nature of these natural systems has driven development of biomimetic approaches. Functionalized gold nanoparticles offer simplified, tunable surfaces that can serve as a proxy to study the reactivity and dynamics of proteins. Amino-acid functionalized gold nanoparticles (Au-TX) served as a complementary partner to cytochrome c (Cyt c) and catalyzed its ET reactivity without altering the native structure. Redox mediator and EPR experiments confirmed that the redox potential and coordination environment …


Investigation Of Fe(Iii) Reduction In Geobacter Sulfurreducens Characterization Of Outer Surface Associated Electron Transfer Components, Xenlei Qian Sep 2009

Investigation Of Fe(Iii) Reduction In Geobacter Sulfurreducens Characterization Of Outer Surface Associated Electron Transfer Components, Xenlei Qian

Open Access Dissertations

Outer membrane cytochromes OmcB and OmcS of Geobacter sulfurreducens are two important components of the respiratory chain for extracellular Fe(III) reduction. OmcS is a loosely bound cell surface protein involved in the reduction of insoluble Fe(III). OmcB is an outer membrane protein and required for insoluble and soluble Fe(III) reduction. The objective of this study was to understand better the mechanism of dissimilatory Fe(III) reduction, focusing on the cell surface proteins by further localization, identification of protein-protein interactions, and biochemical characterization of OmcB and OmcS. OmcB was found to be surface-exposed but embedded in the outer membrane because mild protease …