Protein-Protein Interaction Regulates the Direction of Catalysis and Electron Transfer in a Redox Enzyme Complex.

Protein-protein interactions are well-known to regulate enzyme activity in cell signaling and metabolism. Here, we show that protein-protein interactions regulate the activity of a respiratory-chain enzyme, CymA, by changing the direction or bias of catalysis. CymA, a member of the widespread NapC/NirT superfamily, is a menaquinol-7 (MQ-7) dehydrogenase that donates electrons to several distinct terminal reductases in the versatile respiratory network of Shewanella oneidensis . We report the incorporation of CymA within solid-supported membranes that mimic the inner membrane architecture of S. oneidensis . Quartz-crystal microbalance with dissipation (QCM-D) resolved the formation of a stable complex between CymA and one of its native redox partners, flavocytochrome c3 (Fcc3) fumarate reductase. Cyclic voltammetry revealed that CymA alone could only reduce MQ-7, while the CymA-Fcc3 complex catalyzed the reaction required to support anaerobic respiration, the oxidation of MQ-7. We propose that MQ-7 oxidation in CymA is limited by electron transfer to the hemes and that complex formation with Fcc3 facilitates the electron-transfer rate along the heme redox chain. These results reveal a yet unexplored mechanism by which bacteria can regulate multibranched respiratory networks through protein-protein interactions

Bacterial Power: An Alternative Energy Source

The demand for energy and the limited supply of fossil fuels and their impact in the environment have required the development of alternative energy sources. Among the next generation of energy sources, microbial fuel cells (MFCs) have emerged as a promising technology due to their ability to recover energy from wastewaters in the form of electricity using electroactive microorganisms as catalysts. Among the various factors that affect power generation performance in MFCs, the efficiency of extracellular electron transfer (EET) is one of the most important. Several enzymes, specifically multiheme cytochromes, have been implicated in this process although the electron transfer chain organization remains to be fully understood. In this chapter, we review in detail the mechanisms that support EET from electroactive microorganisms to the anode in MFCs. We focus on the model organism Shewanella oneidensis MR-1, due to the existence of an extensive molecular characterization of its EET processes. The recent developments in the characterization of the multiheme cytochromes involved in these mechanisms will also be reviewed.authorsversionpublishe