Solution structure of mitochondrial cytochrome c. II. 1H nuclear magnetic resonance of ferrocytochrome c.
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Summary
Two-dimensional nuclear magnetic resonance exchange correlated spectroscopy has been used to correlate the assigned resonances of tuna ferricytochrome c with previously unassigned resonancesof tuna ferrocy tochrome c.
- Type
- article
- Published
- 1985-06-05
- Cited by
- 57
- References
- 18
- OpenAlex
- https://openalex.org/W2991532
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:9428820
Keywords
Humanities, Philosophy, Physics, Art
References
- Comparison of the solution and crystal structures of mitochondrial cytochrome c. Analysis of paramagnetic shifts in the nuclear magnetic resonance spectrum of ferricytochrome c.
- 1H NMR studies of the electron exchange between cytochrome c and iron hexacyanides. Definition of the iron hexacyanide binding sites on cytochrome c.
- 1H NMR studies of eukaryotic cytochrome c. Resonance assignments and iron-hexacyanide-mediated electron exchange.
- Nuclear magnetic resonance studies of metal substituted horse cytochrome c
- Proton magnetic resonance evidence for methionine-iron coordination in mammalian-type ferrocytochrome c.
- 1H-NMR studies of structural homologies between the heme environments in horse cytochrome c and in cytochrome c-552 from Euglena gracilis.
- The reaction of cytochrome c with [Fe(EDTA)(H2O)]−
- Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution.
- Nuclear-magnetic-resonance studies of Pseudomonas aeruginosa cytochrome c-551.
- Comparison of the structures of various eukaryotic ferricytochromes c and ferrocytochromes and their antigenic differences.
- Investigation of exchange processes by two‐dimensional NMR spectroscopy
- Structural homology of cytochromes c.
- Proton magnetic resonance studies of horse cytochrome c.
- Spin echo double resonance: a novel method for detecting decoupling in Fourier transform nuclear magnetic resonance
- Correlation of proton chemical shifts in proteins using two-dimensional exchange correlated spectroscopy
- The conformation of eukaryotic cytochrome c around residues 39, 57, 59 and 74.
Cited by
- Comparison of the solution and crystal structures of mitochondrial cytochrome c. Analysis of paramagnetic shifts in the nuclear magnetic resonance spectrum of ferricytochrome c.
- 13C and proton NMR studies of horse cytochrome c
- 13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states.
- NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural alteration on the active site of G. japonicus myoglobin upon azide ion binding.
- 1H NMR studies of 1-methylimidazole complex of cytochrome c
- The role of the internal hydrogen bond network in first-order protein electron transfer between Saccharomyces cerevisiae iso-1-cytochrome c and bovine microsomal cytochrome b5.
- The effects of multiple amino acid substitutions on the polypeptide backbone of tuna and horse cytochromes c.
- Proton NMR studies of two helices in tuna ferricytochrome c.
- 1H and 13C NMR assignment and secondary structure of Chlorobium limicola f. thiosulfatophilum ferrocytochrome c 555
- Mitochondrial control of apoptosis: the role of cytochrome c.
- Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c.
- NMR studies of mobility within protein structure.
- Two-dimensional nuclear magnetic resonance of paramagnetic metalloproteins.
- 1H-NMR sequential assignments and cation-binding studies of spinach plastocyanin.
- Ion binding to cytochrome c.
- 1H NMR studies of azide binding to cytochrome c.
- Proton resonance assignments of horse ferricytochrome c.
- Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect.
- 2D Exsy Studies of γ-Picoline Binding to Cytochrome C
- Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
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