pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thiobacillus yersutus as studied by 300- and 600- MHz 1H NMR.
Open Access
- 1 February 1990
- journal article
- abstracts
- Published by Elsevier
- Vol. 265 (5) , 2768-2774
- https://doi.org/10.1016/s0021-9258(19)39868-0
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- 1H nuclear magnetic resonance study of the protonation behaviour of the histidine residues and the electron self-exchange reaction of azurin from Alcaligenes denitrificansJournal of Molecular Biology, 1988
- Preliminary X-ray crystallographic study of amicyanin from Thiobacillus versutusJournal of Molecular Biology, 1988
- Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH valuesJournal of Molecular Biology, 1986
- Properties of Paracoccus denitrificans amicyaninBiochemistry, 1986
- The pH dependence of the electron self‐exchange rate of azurin from Pseudomonas aeruginosa as studied by 1H‐NMREuropean Journal of Biochemistry, 1985
- Catalysis of plastocyanin electron self‐exchange by redox‐inert multivalent cationsFEBS Letters, 1985
- The assignment of the 1H nuclear magnetic resonance spectrum of azurinEuropean Journal of Biochemistry, 1984
- Connectivity of proton and carbon spectra of the blue copper protein, plastocyanin, established by two‐dimensional nuclear magnetic resonanceFEBS Letters, 1983
- Structure of oxidized poplar plastocyanin at 1·6 Å resolutionJournal of Molecular Biology, 1983
- The effect of pH and temperature on the structure of the active site of azurin from Pseudomonas aeruginosaFEBS Letters, 1982