Literature DB >> 15923154

On the stability of the "wired" bilirubin oxidase oxygen cathode in serum.

Chan Kang1, Hyosul Shin, Adam Heller.   

Abstract

Oxygen is electroreduced to water on the "wired" bilirubin oxidase (w-BOD) catalyst at a considerably lesser potential than on pure platinum. The w-BOD catalyst could be of value in an implantable glucose-O2 biofuel cell, operating living tissue, if it were stable in serum. We found, however, that w-BOD loses its activity in a few hours in the combined presence of the urate and O2, both of which are normal serum constituents (Bioelectrochemistry, 2004, 65, 83-88). Here we report a second major instability: When the disconnected w-BOD cathode is allowed, in the absence of urate, to poise itself at the potential of the O2/H2O half cell at pH 7.2, it loses its activity rapidly. Unlike the urate/O2 caused loss, this loss can be avoided either by applying a potential that is reducing relative to the O2/H2O half-cell potential, or by excluding O2 and adding a mildly reducing reagent, such as urate. The w-BOD cathode can be stored, therefore, in deoxygenated serum, which contains urate.

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Year:  2005        PMID: 15923154     DOI: 10.1016/j.bioelechem.2005.03.002

Source DB:  PubMed          Journal:  Bioelectrochemistry        ISSN: 1567-5394            Impact factor:   5.373


  2 in total

1.  Bilirubin oxidase from Magnaporthe oryzae: an attractive new enzyme for biotechnological applications.

Authors:  Fabien Durand; Sébastien Gounel; Christian H Kjaergaard; Edward I Solomon; Nicolas Mano
Journal:  Appl Microbiol Biotechnol       Date:  2012-02-15       Impact factor: 4.813

2.  A family of Fe-N-C oxygen reduction electrocatalysts for microbial fuel cell (MFC) application: Relationships between surface chemistry and performances.

Authors:  Carlo Santoro; Alexey Serov; Rohan Gokhale; Santiago Rojas-Carbonell; Lydia Stariha; Jonathan Gordon; Kateryna Artyushkova; Plamen Atanassov
Journal:  Appl Catal B       Date:  2017-05-15       Impact factor: 19.503

  2 in total

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