The nature of CuA in cytochrome c oxidase.
Open Access
- 1 October 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (20) , 12106-12113
- https://doi.org/10.1016/s0021-9258(18)33685-8
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- copper proteins systems containing the “Blue” copper centerPublished by Springer Nature ,2007
- Ligand Binding to the blue copper center of horse liver alcohol dehydrogenaseFEBS Letters, 1981
- Mechanism of spin transfer to near neighbors in copper(II) complexesThe Journal of Physical Chemistry, 1980
- Active site-specific reconstituted copper(II) horse liver alcohol dehydrogenase: A biological model for type 1 Cu2+ and its changes upon ligand binding and conformational transitionsJournal of Inorganic Biochemistry, 1980
- The nature of the copper atoms of cytochrome c oxidase as studied by optical and X-ray absorption edge spectroscopyBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1979
- X-ray crystal structure analysis of plastocyanin at 2.7 Å resolutionNature, 1978
- Electron nuclear double resonance on heme compounds. ENDOR from the iron ligands in protohemin chloride and protohemin bromideJournal of the American Chemical Society, 1976
- Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolutionJournal of Molecular Biology, 1976
- Components of cytochrome c oxidase detectable by EPR spectroscopyBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1974
- 460. New syntheses of cystineJournal of the Chemical Society, 1951