Abstract
The weakly coupled 15N atoms around a reduced Rieske [2Fe-2S] cluster of the uniformly 15N-labeled, hyperthermostable archaeal Rieske protein appear to produce readily observable cross-peaks in the HYSCORE spectra, with the well-resolved couplings of 0.3-0.4 MHz for the Nepsilon and 1.1 MHz for the peptide backbone nitrogens, in addition to the contributions from the coordinated Ndelta atoms. These features can be used for structure-mechanism studies of the biological redox protein system involving the weakly coupled nitrogens in coupled electron-proton transfer reactions.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Archaeal Proteins / chemistry*
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Archaeal Proteins / metabolism
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Electron Spin Resonance Spectroscopy / methods
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Electron Transport Complex III / chemistry*
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Electron Transport Complex III / metabolism
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Iron-Sulfur Proteins / chemistry*
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Iron-Sulfur Proteins / metabolism
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Nitrogen Isotopes
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Sulfolobus / chemistry
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Sulfolobus / metabolism
Substances
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Archaeal Proteins
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Iron-Sulfur Proteins
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Nitrogen Isotopes
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Rieske iron-sulfur protein
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Electron Transport Complex III