Literature DB >> 4978609

The mechanism of laccase-catalyzed oxidations: kinetic evidence for the involvement of several electron-accepting sites in the enzyme.

B G Malmström, A F Agrò, E Antonini.   

Abstract

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Year:  1969        PMID： 4978609     DOI： 10.1111/j.1432-1033.1969.tb00620.x

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


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  7 in total

Review 1.  Co-operation of electron-accepting sites in oxygen reduction by oxidases.

Authors:  B G Malmström
Journal:  Biochem J       Date:  1970-04       Impact factor: 3.857

2.  [The phenoloxidases of the ascomycete Podospora anserina. V. Properties of laccase I after further purification].

Authors:  H P Molitoris; K Esser
Journal:  Arch Mikrobiol       Date:  1970

3.  The phenol oxidases of the ascomycete Podospora anserina. XII. Affinity of laccases II and III to substrates with different substitution patterns.

Authors:  P Hoffmann; K Esser
Journal:  Arch Microbiol       Date:  1977-02-04       Impact factor: 2.552

4.  Pulse-radiolysis studies on the interaction of one-electron reduced species with blue oxidases. Reduction of type-2-copper-depleted ascorbate oxidase.

Authors:  P O'Neill; E M Fielden; L Avigliano; G Marcozzi; A Ballini; F Agrò
Journal:  Biochem J       Date:  1984-08-15       Impact factor: 3.857

5.  Anaerobic reactions of Rhus vernicifera laccase and its type-2 copper-depleted derivatives with hexacyanoferrate(II).

Authors:  T Sakurai
Journal:  Biochem J       Date:  1992-06-15       Impact factor: 3.857

6.  Pulse-radiolysis studies on the interaction of one-electron-reduced species with ascorbate oxidase in aqueous solution.

Authors:  P O'Neill; E M Fielden; A Finazzi-Agrò; L Avigliano
Journal:  Biochem J       Date:  1983-01-01       Impact factor: 3.857

7.  Eraldo Antonini Lectures, 1983-2019.

Authors:  Maurizio Brunori
Journal:  Biol Direct       Date:  2022-07-15       Impact factor: 7.173
  7 in total

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