Journal article

Structural basis of interprotein electron transfer in bacterial sulfite oxidation

Aaron P McGrath, Elise L Laming, G Patricia Casas Garcia, Marc Kvansakul, J Mitchell Guss, Jill Trewhella, Benoit Calmes, Paul V Bernhardt, Graeme R Hanson, Ulrike Kappler, Megan J Maher



Interprotein electron transfer underpins the essential processes of life and relies on the formation of specific, yet transient protein-protein interactions. In biological systems, the detoxification of sulfite is catalyzed by the sulfite-oxidizing enzymes (SOEs), which interact with an electron acceptor for catalytic turnover. Here, we report the structural and functional analyses of the SOE SorT from Sinorhizobium meliloti and its cognate electron acceptor SorU. Kinetic and thermodynamic analyses of the SorT/SorU interaction show the complex is dynamic in solution, and that the proteins interact with Kd = 13.5 ± 0.8 μM. The crystal structures of the oxidized SorT and SorU, both in isolatio..

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University of Melbourne Researchers


Awarded by Australian Research Council

Awarded by National Health and Medical Research Council

Funding Acknowledgements

Australian Research Council Discovery Project Grant DP0878525 Ulrike Kapplerr National Health and Medical Research Council CJ Martin Postdoctoral Research Fellowship 1053624 Aaron P McGrathr Australian Research Council Discovery Project Grant DP1211465 Paul V Bernhardtr The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.