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Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551

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Abstract

Hydrogen exchange rates for backbone amide protons of oxidized Pseudomonas aeruginosa cytochrome c-551 (P. aeruginosa cytochrome c) have been measured in the presence of low concentrations of the denaturant guanidine hydrochloride. Analysis of the data has allowed identification of submolecular unfolding units known as foldons. The highest-energy foldon bears similarity to the proposed folding intermediate for P. aeruginosa cytochrome c. Parallels are seen to the foldons of the structurally homologous horse cytochrome c, although the heme axial methionine-bearing loop has greater local stability in P. aeruginosa cytochrome c, in accord with previous folding studies. Regions of low local stability are observed to correspond with regions that interact with redox partners, providing a link between foldon properties and function.

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Acknowledgments

This work is supported by NIH grant R01-GM63170.

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Authors and Affiliations

  1. Department of Biochemistry and Biophysics, University of Rochester, Rochester, NY, 14642, USA

    Lea V. Michel

  2. Department of Chemistry, University of Rochester, Rochester, NY, 14627-0216, USA

    Kara L. Bren

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  1. Lea V. Michel
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  2. Kara L. Bren
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Correspondence to Kara L. Bren.

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Michel, L.V., Bren, K.L. Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551. J Biol Inorg Chem 13, 837–845 (2008). https://doi.org/10.1007/s00775-008-0370-y

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  • DOI: https://doi.org/10.1007/s00775-008-0370-y

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