Literature DB >> 1847342

Triiodide reduction by cellobiose:quinone oxidoreductase of Phanerochaete chrysosporium.

W J Bao1, V Renganathan.   

Abstract

Cellobiose:quinone oxidoreductase (CBQase) in the presence of cellobiose inhibits peroxidase-catalyzed oxidation of iodide to triiodide (I3). This inhibition is due to the two-electron reduction of I3- by CBQase. The apparent Km of I3- for this reaction is 120 microM and the specific activity is 57 mumol.min-1.mg-1. A proposed mechanism for I3- reduction by CBQase involves initial reduction of the flavin moiety by cellobiose to produce a dihydroflavin. This is followed by the substitution of one of the iodine atoms of I3- at the C(4a)-position of dihydroflavin to generate C(4a)-iododihydroflavin and two iodide ions. The C(4a)-iododihydroflavin eliminates HI to regenerate the oxidized CBQase.

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Year:  1991        PMID: 1847342     DOI: 10.1016/0014-5793(91)80242-u

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1.

Authors:  G Henriksson; A Salumets; C Divne; G Pettersson
Journal:  Biochem J       Date:  1997-06-15       Impact factor: 3.857

2.  Novel interaction between laccase and cellobiose dehydrogenase during pigment synthesis in the white rot fungus Pycnoporus cinnabarinus.

Authors:  U Temp; C Eggert
Journal:  Appl Environ Microbiol       Date:  1999-02       Impact factor: 4.792

Review 3.  Bioconversion of lignocellulose materials.

Authors:  C Pothiraj; P Kanmani; P Balaji
Journal:  Mycobiology       Date:  2006-12-31       Impact factor: 1.858

  3 in total

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