Connectivity of proton and carbon spectra of the blue copper protein, plastocyanin, established by two‐dimensional nuclear magnetic resonance
- 3 October 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 162 (1), 52-56
- https://doi.org/10.1016/0014-5793(83)81047-3
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Heteronuclear (proton, carbon-13) two-dimensional chemical shift correlation NMR spectroscopy of a protein. Ferredoxin from Anabaena variabilisJournal of the American Chemical Society, 1982
- A two-dimensional NMR method for assignment of imidazole ring proton resonances of histidine residues in proteinsBiochemical and Biophysical Research Communications, 1982
- Two‐Dimensional NMR Spectroscopy of Siomycin AEuropean Journal of Biochemistry, 1982
- Dependence of NMR lineshape analysis upon chemical rates and mechanisms: Implications for enzyme histidine titrationsJournal of Magnetic Resonance (1969), 1980
- NMR study of the interaction of plastocyanin with chromium(III) analogues of inorganic electron transfer reagentsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1980
- Electron transfer reagent binding sites on plastocyaninNature, 1980
- High resolution proton magnetic resonance studies of plastocyaninFEBS Letters, 1978
- Nuclear magnetic resonance studies of the copper binding sites of blue copper proteins. Oxidized, reduced, and apoplastocyaninBiochemistry, 1975
- The kinetics and specificity of electron transfer from cytochromes and copper proteins to P700Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
- Observation of histidine residues in proteins by nuclear magnetic resonance spectroscopyAccounts of Chemical Research, 1975