Submolecular unfolding units of <Emphasis Type="Italic">Pseudomonas aeruginosa</Emphasis> cytochrome <Emphasis Type="Italic">c</Emphasis>-551 |
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Authors: | Lea V Michel Kara L Bren |
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Institution: | (1) Department of Biochemistry and Biophysics, University of Rochester, Rochester, NY 14642, USA;(2) Department of Chemistry, University of Rochester, Rochester, NY 14627-0216, USA |
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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.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. |
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Keywords: | Cytochrome Denaturant Electron transfer Heme Nuclear magnetic resonance |
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