copper proteins systems containing the “Blue” copper center

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• Publication year

  1975

• Venue

  Unknown venue

• Publication date

  Unknown publication date

• Fields of study

  Biology, Chemistry

• Identifiers
  DOI 10.1007/BFB0116549
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

• Purification and properties of crystalline human ceruloplasmin.

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• Sulfhydryl groups, disulfide bridges and the state of copper in three blue oxidases

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• Circular dichroism of disulfides with dihedral angles of 0, 30, and 60.deg. in the 400-185nm spectral region

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• The stoichiometry of the three different types of copper in ascorbate oxidase from green zucchini squash

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• Concerning the quaternary structure of ascorbate oxidase.

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• Resonance Raman studies of "blue" copper proteins.

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• Binding of water to "types I and II" Cu2+ in proteins.

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• The amino acid sequence of plastocyanin from Solanum tuberosum L. (potato).

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• Mechanistic studies of the reduction of Rhus vernicifera laccase by hydroquinone.

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• The effect of fluoride on the spectral and catalytic properties of the three copper-containing oxidases.

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• An intermediate in the reaction of reduced laccase with oxygen

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• Disulfide bond dihedral angles from Raman spectroscopy.

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• Effect of pH on electron-paramagnetic-resonance spectra of ceruloplasmin.

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• Anion-binding and the state of copper in caeruloplasmin.

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• Kinetic studies on the aerobic oxidation of reduced human ceruloplasmin.

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• The association of the copper derived from ceruloplasmin with cytocuprein.

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• Kinetics of the interaction between ceruloplasmin and reducing substrates.

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• The kinetics of the anaerobic reduction of fungal laccase B.

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• The reaction of nitric oxide with ceruloplasmin.

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• The Amino Acid Sequence of Chlorella fusca Plastocyanin

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• Luminescence quenching in azurin.

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• The ratio of type-I and -2 Cu(II) in human ceruloplasmin.

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• Dissociation and reconstitution of human ceruloplasmin.

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• The oxidation-reduction potential of membrane-bound chloroplast plastocyanin and cytochrome f.

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• The stoichiometry of the paramagnetic copper and the oxidation-reduction potentials of type I copper in human ceruloplasmin.

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• Inhibition of ceruloplasmin by inorganic anions.

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• Conformational dependence of the electronic energy levels in disulfides

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• Evidence for proteolytic fragments in commercial samples of human ceruloplasmin

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• Evidence of a specific copper(II) in human ceruloplasmin as a binding site for inhibitory anions.

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• Role of iron in the oxidase activity of ceruloplasmin.

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• The requirement of the “non‐blue” copper (II) for the activity of fungal laccase

  1968cited by this paper
• Cupric ion in blue proteins.

  1968cited by this paper

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