Redox Potentials of the Flavoprotein Lactate Oxidase

  • Stankovich M
  • Fox B
  • 4


    Mendeley users who have this article in their library.
  • 44


    Citations of this article.


The redox potentials for both electron transfers for the enzyme lactate oxidase have been measured at pH 7.0 in 0.01 M imidazole buffer at 25 degrees C. Methylviologen is the electrochemically generated reducing agent capable of transferring both electrons to the enzyme in this spectroelectrochemical experiment. The E0' values are as follows: for EFlox + e- = EFl-., E0'1 = -0.067 +/- 0.006 V; for EFl-. + e- + H+ = EFlredH-, E0'2 = -0.231 +/- 0.004 V. All potentials are reported vs. the standard hydrogen electrode (SHE). Both electron transfers are reversible. Consistent with the 164-mV potential separation, 95% of the enzyme anion radical is thermodynamically stabilized at half-reduction in all experiments.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Marian Stankovich

  • Brian Fox

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free