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Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
Decavanadate interacts with microsomal NADH oxidation system and enhances cytochrome c reduction
1Centre for DNA Fingerprinting & Diagnostics, Hyderabad 500 076, India. trs@cdfd.org.in
Molecular and Cellular Biochemistry
|December 6, 2005
Summary
Decavanadate (DV) acts as an electron acceptor in microsomal systems, facilitating NADH oxidation and oxygen consumption. This vanadate species shows potential as a redox intermediate in biological electron transport chains.
Area of Science:
- Biochemistry
- Biophysics
- Enzyme kinetics
Background:
- Microsomal systems are crucial for cellular redox reactions.
- Vanadates are known to interact with biological systems.
- NADH oxidation is a key metabolic process linked to oxygen consumption.
Purpose of the Study:
- To investigate the role of metavanadate (MV) and decavanadate (DV) in NADH oxidation.
- To determine if DV can act as an electron acceptor in microsomal systems.
- To characterize the redox properties of DV in relation to NADH oxidation.
Main Methods:
- Spectrophotometric monitoring of NADH oxidation and oxygen consumption.
- Incubation of microsomes with MV and DV.
- Assessment of DV reduction and its spectral properties.
- Evaluation of DV's effect on cytochrome c reduction.
Main Results:
- NADH oxidation and oxygen consumption (1:1 ratio) occurred with MV and DV.
- DV was reduced to a vanadyl-V(IV) form with distinct spectral properties.
- DV functioned as an electron acceptor, similar to ferricyanide and cytochrome c.
- DV significantly enhanced the rate of cytochrome c reduction at micromolar concentrations.
Conclusions:
- Decavanadate acts as an effective electron acceptor in microsomal NADH oxidation.
- DV exhibits potential as a redox intermediate in biological electron transport.
- The observed vanadyl-V(IV) species possesses unique spectral characteristics.
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