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Determining Rieske cluster reduction potentials

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Abstract

The Rieske iron–sulfur proteins have reduction potentials ranging from −150 to +400 mV. This enormous range of potentials was first proposed to be due to differing solvent exposure or even protein structure. However, the increasing number of available crystal structures for Rieske iron–sulfur proteins has shown this not to be the case. Colbert and colleagues proposed in 2000 that differences in the electrostatic environment, and not structural differences, of a Rieske proteins are responsible for the wide range of reduction potentials observed. Using computational simulation methods and the newly determined structure of Pseudomonas sp. NCIB 9816-4 naphthalene dioxygenase Rieske ferredoxin (NDO-F9816-4), we have developed a model to predict the reduction potential of Rieske proteins given only their crystal structure. The reduction potential of NDO-F9816-4, determined using a highly oriented pyrolytic graphite electrode, was −150 ± 2 mV versus the standard hydrogen electrode. The predicted reduction potentials correlate well with experimentally determined potentials. Given this model, the effect of protein mutations can be evaluated. Our results suggest that the reduction potential of new proteins can be estimated with good confidence from 3D structures of proteins. The structure of NDO-F9816-4 is the most basic Rieske ferredoxin structure determined to date. Thus, the contributions of additional structural motifs and their effects on reduction potential can be compared with respect to this base structure.

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Acknowledgments

We thank Dan Ferraro, Adam Okerlund, Lokesh Gakhar, Chi-Li Yu, Johna Leddy, David Gibson, and Hans Eklund for their support, ideas, and assistance. We thank Elizabeth Kamp for her assistance in editing this manuscript. We would like to thank the Macromolecular Crystallography Group beamline ID14-1 at the European Synchrotron Radiation Facility for help with data collection. E.B. is a University of Iowa MSTP trainee and would like to acknowledge financial support through a fellowship from the University of Iowa Center for Biocatalysis and Bioprocessing. M.M.J.C. was the recipient of a studentship from the FCAR of Quebec, Canada. S.R. would like to acknowledge financial support from USPHS grant no. GM62904. This work was supported in part by a Discovery grant from the Natural Sciences and Engineering Research Council (NSERC) of Canada (to L.D.E.).

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Authors and Affiliations

  1. Department of Biochemistry, University of Iowa, Iowa City, IA, 52242, USA

    Eric N. Brown & S. Ramaswamy

  2. Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, Uppsala, Sweden

    Rosmarie Friemann & Andreas Karlsson

  3. Section of Microbiology, University of California, Davis, CA, 95616, USA

    Juan V. Parales

  4. Medicago R&D, 1020 route de l’Eglise, Ste-Foy, QC, G1V 3V9, Canada

    Manon M.-J. Couture

  5. Department of Microbiology and Immunology, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada

    Lindsay D. Eltis

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  1. Eric N. Brown
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Correspondence to S. Ramaswamy.

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Brown, E.N., Friemann, R., Karlsson, A. et al. Determining Rieske cluster reduction potentials. J Biol Inorg Chem 13, 1301–1313 (2008). https://doi.org/10.1007/s00775-008-0413-4

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