ArticleJournal of the American Chemical Society2009
Hyperfine-shifted (13)C and (15)N NMR signals from Clostridium pasteurianum rubredoxin: extensive assignments and quantum chemical verification.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- OptimizedInternational journal of molecular sciences · 2025Article
- Paramagnetic NMR to study iron sulfur proteins:Journal of biomolecular NMR · 2023Article
- Review
- A Quantum Chemistry View on Two Archetypical Paramagnetic Pentacoordinate Nickel(II) Complexes Offers a Fresh Look on Their NMR Spectra.Inorganic chemistry · 2021Article
- Measuring transverse relaxation in highly paramagnetic systems.Journal of biomolecular NMR · 2020Article
- Biomolecular NMR: Past and future.Archives of biochemistry and biophysics · 2017Article
- The IR-¹⁵N-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules.Journal of biomolecular NMR · 2014Article
- FeoC from Klebsiella pneumoniae contains a [4Fe-4S] cluster.Journal of bacteriology · 2013Article
- Accurate structure and dynamics of the metal-site of paramagnetic metalloproteins from NMR parameters using natural bond orbitals.Journal of the American Chemical Society · 2012Article
- Speeding up direct (15)N detection: hCaN 2D NMR experiment.Journal of biomolecular NMR · 2011Article
- Spectroscopy: Unexpected interactions.Nature · 2011Article
- Hyperfine-shifted 13C resonance assignments in an iron-sulfur protein with quantum chemical verification: aliphatic C-H···S 3-center-4-electron interactions.Journal of the American Chemical Society · 2011Article
- Nitrogen-detected CAN and CON experiments as alternative experiments for main chain NMR resonance assignments.Journal of biomolecular NMR · 2010Article
- An NMR structural study of nickel-substituted rubredoxin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
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6 authors.
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Abstract
Stable isotope-labeling methods, coupled with novel techniques for detecting fast-relaxing NMR signals, now permit detailed investigations of paramagnetic centers of metalloproteins. We have utilized these advances to carry out comprehensive assignments of the hyperfine-shifted (13)C and (15)N signals of the rubredoxin from Clostridium pasteurianum (CpRd) in both its oxidized and reduced states. We used residue-specific labeling (by chemical synthesis) and residue-type-selective labeling (by biosynthesis) to assign signals detected by one-dimensional (15)N NMR spectroscopy, to nitrogen atoms near the iron center. We refined and extended these (15)N assignments to the adjacent carbonyl carbons by means of one-dimensional (13)C[(15)N] decoupling difference experiments. We collected paramagnetic-optimized SuperWEFT (13)C[(13)C] constant time COSY (SW-CT-COSY) data to complete the assignment of (13)C signals of reduced CpRd. By following these (13)C signals as the protein was gradually oxidized, we transferred these assignments to carbons in the oxidized state. We have compared these assignments with hyperfine chemical shifts calculated from available X-ray structures of CpRd in its oxidized and reduced forms. The results allow the evaluation of the X-ray structural models as representative of the solution structure of the protein, and they provide a framework for future investigation of the active site of this protein. The methods developed here should be applicable to other proteins that contain a paramagnetic center with high spin and slow electron exchange.
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