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Protein dynamics and cytochrome c: Correlations between ligand vibrations and redox activity

Academic Article
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Overview

authors

  • Chin, J. K.
  • Jimenez, R.
  • Romesberg, Floyd

publication date

  • March 2002

journal

  • Journal of the American Chemical Society  Journal

abstract

  • A recently developed method to directly observe specific protein vibrations, based on deuteration, has been employed to examine the redox-dependent structural and fluctional properties of cytochrome c. The dynamics of the protein-based methionine heme ligand were examined by selectively deuterating the ligand's methyl group. The frequency and line width of the C-D bonds were easily observable and shown to be sensitive to mutation-induced changes in the protein redox potential. However, of seven mutants examined, the C-D line widths were independent of the redox-state of the protein. Therefore, although the ligand dynamics depend on the protein's redox state, there are no detected differences in protein dynamics of the oxidized and reduced proteins.

subject areas

  • Cytochrome c Group
  • Deuterium
  • Ferrous Compounds
  • Ligands
  • Models, Molecular
  • Oxidation-Reduction
  • Protein Conformation
  • Vibration
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja012312n

PubMed ID

  • 11866585
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Additional Document Info

start page

  • 1846

end page

  • 1847

volume

  • 124

issue

  • 9

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