Literature DB >> 2373076

The role of copper in the stability of ascorbate oxidase towards denaturing agents.

I Savini1, S D'Alessio, A Giartosio, L Morpurgo, L Avigliano.   

Abstract

The susceptibility of native, type-2 Cu-depleted and fully Cu-depleted ascorbate oxidase to thermal and chemical denaturation has been probed by differential scanning calorimetry, fluorimetry and circular dichroism. The data indicate that copper affects the stability, but not the protein conformation. The unfolding of ascorbate oxidase is characterized by a single endotherm. Calorimetric domains revealed by deconvolution are consistent with the domains identified by X-ray crystallography.

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Year:  1990        PMID： 2373076     DOI： 10.1111/j.1432-1033.1990.tb15600.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


  7 in total

1.  The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability.

Authors:  André T Fernandes; Manuela M Pereira; Catarina S Silva; Peter F Lindley; Isabel Bento; Eduardo Pinho Melo; Lígia O Martins
Journal:  J Biol Inorg Chem       Date:  2011-03-03       Impact factor: 3.358

Review 2.  Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.

Authors:  Lígia O Martins; Paulo Durão; Vânia Brissos; Peter F Lindley
Journal:  Cell Mol Life Sci       Date:  2015-01-09       Impact factor: 9.261

3.  Stability of Japanese-lacquer-tree (Rhus vernicifera) laccase to thermal and chemical denaturation: comparison with ascorbate oxidase.

Authors:  E Agostinelli; L Cervoni; A Giartosio; L Morpurgo
Journal:  Biochem J       Date:  1995-03-15       Impact factor: 3.857

4.  Copper incorporation into recombinant CotA laccase from Bacillus subtilis: characterization of fully copper loaded enzymes.

Authors:  Paulo Durão; Zhenjia Chen; André T Fernandes; Peter Hildebrandt; Daniel H Murgida; Smilja Todorovic; Manuela M Pereira; Eduardo P Melo; Lígia O Martins
Journal:  J Biol Inorg Chem       Date:  2007-10-24       Impact factor: 3.358

5.  Role of copper in thermal stability of human ceruloplasmin.

Authors:  Erik Sedlák; Gabriel Zoldák; Pernilla Wittung-Stafshede
Journal:  Biophys J       Date:  2007-10-26       Impact factor: 4.033

6.  In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site.

Authors:  Erik Sedlák; Lynn Ziegler; Daniel J Kosman; Pernilla Wittung-Stafshede
Journal:  Proc Natl Acad Sci U S A       Date:  2008-11-25       Impact factor: 11.205

7.  Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.

Authors:  Erik Sedlák; Gabriel Žoldák; Pernilla Wittung-Stafshede
Journal:  Int J Mol Sci       Date:  2018-01-16       Impact factor: 5.923
  7 in total

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