Comparison of amide proton exchange in reduced and oxidizedRhodobacter capsulatus cytochrome c2: A1H−15N NMR study
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Summary
The difference in NH exchange rates between the redox states for a number of residues including His17, Leu37, Arg43, Ala45, Gly46, Ile57, Val58,Leu60, Gly61 and Leu100 suggest that interactions affecting the causes of these differences may be important factors in determining redox potential.
- Type
- article
- Published
- 1991-07-01
- Cited by
- 19
- References
- 19
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- https://openalex.org/W1668720
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Keywords
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References
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Cited by
- Multidimensional nuclear magnetic resonance methods to probe metal environments in proteins.
- Redox-dependent dynamics in cytochrome P450cam
- Isotope labeling in solution protein assignment and structural analysis
- Hydrogen exchange and protein folding.
- Protein stability parameters measured by hydrogen exchange
- Conformational properties of Rhodobacter capsulatus cytochrome c2 wild‐type and site‐directed mutants using hydrogen/deuterium exchange monitored by electrospray ionization mass spectrometry
- Experimental study of the protein folding landscape: unfolding reactions in cytochrome c.
- Site-specific mutagenesis studies of cytochromes c.
- Redox‐dependent dynamics of putidaredoxin characterized by amide proton exchange
- Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin. Relation to the structure of the putative binding site and the cytolytic activity of the toxin.
- An optimized g‐tensor for rhodobacter capsulatus cytochrome c2 in solution: A structural comparison of the reduced and oxidized states
- Amide proton exchange rates of oxidized and reduced saccharomyces cerevisiae iso‐1‐cytochrome c
- Assignment of the 13C and 13CO resonances for Rhodobacter capsulatus ferrocytochrome c2 using double-resonance and triple-resonance NMR spectroscopy.
- Stability study of Rhodobacter capsulatus ferrocytochrome c 2 wild‐type and site‐directed mutants using hydrogen/deuterium exchange monitored by electrospray ionization mass spectrometry
- Redox‐related conformational changes in Rhodobacter capsulatus cytochrome c2
- Mapping the effects of metal ion reduction and substrate analog binding to Fe‐superoxide dismutase by NMR spectroscopy †
- Determinants of protein hydrogen exchange studied in equine cytochrome c
- Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers
- Chapter 3 – Preperation of 2H, 13C and 15N Isotopically-enriched Proteins for NMR Spectroscopic Investigations
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