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Updated: Jun 13, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
Kinetics of myoglobin redox form stabilization by malate dehydrogenase
Anand Mohan1, S Muthukrishnan, Melvin C Hunt
1Department of Animal Sciences and Industry, Weber Hall, Kansas State University, 224 Weber Hall, Manhattan, Kansas 66506, USA.
Abstract:
This study reports the reduction of metmyoglobin (MMb) via oxidation of malate to oxaloacetate and the regeneration of reduced nicotinamide adenine dinucleotide (NADH) via malate dehydrogenase (MDH). Two experiments were conducted to evaluate a malate-MDH-NADH system as a possible mechanism for MMb reduction. In experiment 1, kinetics of MDH and MMb reduction were determined, and the results showed that increasing concentrations of oxidized nicotinamide adenine dinucleotide (NAD(+)) and l-malate also increased (p < 0.05) MMb reduction in vitro. Experiment 2 assessed the reducing activity of beef muscle extracts with different concentrations of malate and NAD(+) added. Reduction of MMb in the muscle extracts via MDH was NAD(+), malate, and extract concentration dependent (p < 0.05). A new mechanism is described for the nonspecific and specific enzymatic reduction of MMb, which supports the hypothesis that malate can replenish NADH via MDH activity in post-mortem muscle, ultimately resulting in a more functional meat color.
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