13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states.
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Summary
Comparison of the paramagnetic shifts of carbon and protons indicates a small redox-related change of conformation in the vicinity of Trp59 and a significant expansion of the protein over 30-50 degrees C.
- Type
- article
- Published
- 1992-06-01
- Cited by
- 39
- References
- 16
- Access
- Open access
- OpenAlex
- https://openalex.org/W1910174567
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:41158297
Keywords
Chemistry, Proton, Chemical shift, Proton NMR, Carbon-13 NMR
References
- Solution structure of mitochondrial cytochrome c. II. 1H nuclear magnetic resonance of ferrocytochrome c.
- NMR in biological research: Peptides and proteins
- 13C and proton NMR studies of horse cytochrome c
- Two-Dimensional 1H13C chemical-shift correlated spectroscopy of a protein at natural abundance
- Distortionless enhancement of NMR signals by polarization transfer
- Cross-correlation of spin-decoupled NMR spectra by heteronuclear two-dimensional spectroscopy
- Proton resonance assignments of horse ferricytochrome c.
- Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution.
- Basic two-dimensional NMR
- Cytochrome c: observation of numerous single-carbon sites of the reduced and oxidized species by means of natural-abundance 13C nuclear magnetic resonance spectroscopy.
- Experimental chemical shift correlation maps in nuclear magnetic resonance spectroscopy
- Investigation of exchange processes by two‐dimensional NMR spectroscopy
- The magnetic susceptibility of ferricytochrome c
- A systematic approach towards the complete assignment of 13C resonances for horse ferrocytochrome c.
- 13C‐NMR studies of horse ferrocytochrome c
Cited by
- Two-dimensional nuclear magnetic resonance spectra of paramagnetic systems.
- Determination of Haem Electronic Structure in His‐Met Cytochromes c by 13C‐NMR
- Protein stability and mutations in the axial methionine loop of a minimal cytochrome c
- 1H NMR studies of paramagnetic ferricytochrome c-551 from Pseudomonas aeruginosa at high pH: The role of histidine 16 in the spin transition
- Characteristics of the paramagnetic 1H-NMR spectra of the ferricytochrome c-551 family.
- Isotope labeling in solution protein assignment and structural analysis
- Ligand orientation and haem electronic structure in ferricytochrome c′′ from Methylophilus methylotrophus studied by 13C NMR
- Recent developments in the 13C NMR spectroscopic analysis of paramagnetic hemes and heme proteins
- Two-dimensional nuclear magnetic resonance of paramagnetic metalloproteins.
- Heteronuclear multiple-quantum coherence NMR spectroscopy of IM-CYTC
- Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila.
- Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfovibrio vulgaris.
- Carbon‐13 NMR study of the B9(Asp) mutant of human insulin: Sequence‐specific carbon‐13 assignments and structural information
- Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure.
- 1H one-dimensional and two-dimensional NMR studies of the ferricytochrome c 551 from Rhodocyclus gelatinosus.
- The Conformational Flexibility of Oxidized Cytochrome c Studied through Its Interaction with NH3 and at High Temperatures
- Determination of haem electronic structure in cytochrome b5 and metcyanomyoglobin.
- Evaluation of 13C and 1H Fermi contact shifts in horse cytochrome c. The origin of the anti-Curie effect.
- Copper-zinc superoxide dismutase: A paramagnetic protein that provides a unique frame for the NMR investigation
- Isolation and characterization of cytochrome c2 from Rhodopseudomonas palustris
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