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Literature summary for 1.3.3.5 extracted from

  • Filip, J.; Tkac, J.
    The pH dependence of the cathodic peak potential of the active sites in bilirubin oxidase (2014), Bioelectrochemistry, 96, 14-20 .
    View publication on PubMed
Search for more literature for 1.3.3.5

Protein Variants

Protein Variants Comment Organism
additional information enzyme immobilization on an electrode, bilirubin oxidase adsorbed on a nanocomposite modified electrode has three distinct redox sites within that show pH dependence: the 1st redox centre with the highest redox potential Ec(1st) = 404 mV vs. Ag/AgCl (614 mV vs. NHE at pH 7.0) exhibits pH dependence with a slope -dEc(1st)/dpH = 66 mVunder a non-turnover process. The 2nd redox centre with a potential Ec(2nd) = 228 mV vs. Ag/AgCl (438 mV vs. NHE at pH 7.0) is not dependent on pH in the absence and presence of O2. Finally, the 3rd redox site with a redox potential Ec(3rd) = 92 mVvs. Ag/AgCl (302 mV vs. NHE at pH 7.0) exhibits pH dependence for a cathodic process with -dEc(3rd)/dpH = 70 mV and for anodic process with -dEa(3rd)/dpH = 73 mV, respectively. Two break points for dependence of Ec(1st) or Ec(3rd) on pH are observed for the 1st (T1) site and the 3rd site assigned to involvement of two acidic amino acids, Asp105 and Glu463. Potential difference between cathodic peaks of BOD as a dependence on pH, overview Albifimbria verrucaria

Organism

Organism UniProt Comment Textmining
Albifimbria verrucaria Q12737
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-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Albifimbria verrucaria
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Synonyms

Synonyms Comment Organism
BOD
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 Albifimbria verrucaria

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4 6 assay at Albifimbria verrucaria

pH Range

pH Minimum pH Maximum Comment Organism
4 9 analysis of pH dependence of the enzyme immobilized on electrodes, detailed overview Albifimbria verrucaria