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J. Biol. Chem., Vol. 281, Issue 20, 99913, May 19, 2006

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Electron Transfer from One Protein to Another

Model of the complex between cytochrome c552 and the ba3 oxidase.

The conduits by which electrons are transferred between two metalloproteins have been extensively studied by both theoretical and experimental approaches for the last decade. Despite this effort, there are very few cases where the electron transfer pathways are established. In this Paper of the Week, Lucia Muresanu and colleagues utilize the power of high field NMR spectroscopy to establish a highly plausible route through which electron transfer occurs from the heme center of a c-type cytochrome to its partner copper center of a terminal oxidase. The work includes the use of thermostable protein partners, advanced NMR spectroscopic methods, and sophisticated analysis to establish a plausible model for the electron transfer partner complex.

Using NMR-based chemical shift perturbation mapping, the researchers identified the contact regions between the redox complex of the soluble cytochrome c₅₅₂ and the membrane-integral cytochrome ba₃ oxidase of Thermus thermophilus. Chemical shift analysis provided a topographical description of the contact surface on each partner molecule. A protein-protein docking calculation was then preformed to produce a structure ensemble of 10 closely related conformers representing the complex between the cytochromes. Based on these structures, Muresanu et al. predicted the electron transfer pathway from the heme of cytochrome c₅₅₂ to the Cu_A center of the ba₃ oxidase.

FOOTNOTES

See referenced article, J. Biol. Chem. 2006, 281, 14503-14513

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Related Collections Papers Of The Week Social Bookmarking                      What's this?