Mutation of the heme-binding crevice of flavocytochrome b2 from Saccharomyces cerevisiae: altered heme potential and absence of redox cooperativity between heme and FMN centers.

Abstract excerpt

Kinetic and thermodynamic properties of yeast flavocytochrome b2 (EC 1.1.2.3) are modified by the product pyruvate, which binds to the flavosemiquinone (FSQ) form of the prosthetic flavin and decreases the thermodynamic driving force for electron transfer from FSQ to heme. Pyruvate inhibits flavocytochrome b2, but the catalytic competence of pyruvate-ligated FSQ in intramolecular electron transfer to heme is...

Topics

• Base Sequence
• Flavin Mononucleotide
• Heme
• Kinetics
• L-Lactate Dehydrogenase
• L-Lactate Dehydrogenase (Cytochrome)
• Molecular Sequence Data
• Mutation
• Oligonucleotides
• Oxidation-Reduction
• Potentiometry