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Transition metal complexes as mediator-titrants in protein redox potentiometry

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Abstract

A selection of nine macrocyclic FeIII/II and CoIII/II transition metal complexes has been chosen to serve as a universal set of mediator-titrants in redox potentiometry of protein samples. The potential range spanned by these mediators is approximately from +300 to −700 mV vs the normal hydrogen electrode, which covers the range of most protein redox potentials accessible in aqueous solution. The complexes employed exhibit stability in both their oxidized and their reduced forms as well as pH-independent redox potentials within the range 6 < pH < 9. The mediators were also chosen on the basis of their very weak visible absorption maxima in both oxidation states, which will enable (for the first time) optical redox potentiometric titrations of proteins with relatively low extinction coefficients. This has previously been impractical with organic mediators, such as indoles, viologens and quinones, whose optical spectra interfere strongly with those of the protein.

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Abbreviations

EPR:

Electron paramagnetic resonance

NHE:

Normal hydrogen electrode

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Acknowledgements

We gratefully acknowledge financial support from the Australian Research Council (DP0343405). We also thank L.R. Gahan for a generous gift of [Co(AMME-N5S-sar)]Cl3 and [Co(CLME-N4S2-sar)]Cl3.

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Authors and Affiliations

  1. Centre for Metals in Biology, Department of Chemistry, University of Queensland, Brisbane, 4072, QLD, Australia

    Paul V. Bernhardt, Kuan-I. Chen & Philip C. Sharpe

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  1. Paul V. Bernhardt
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  2. Kuan-I. Chen
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  3. Philip C. Sharpe
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Correspondence to Paul V. Bernhardt.

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Bernhardt, P.V., Chen, KI. & Sharpe, P.C. Transition metal complexes as mediator-titrants in protein redox potentiometry. J Biol Inorg Chem 11, 930–936 (2006). https://doi.org/10.1007/s00775-006-0148-z

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  • DOI: https://doi.org/10.1007/s00775-006-0148-z

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