Bianchi 2003 Biofactors
| Bianchi C, Fato R, Genova ML, Parenti Castelli F, Lenaz G (2003) Structural and functional organization of Complex I in the mitochondrial respiratory chain. Biofactors 18:3-9. |
Bianchi C, Fato R, Genova ML, Parenti Castelli F, Lenaz G (2003) Biofactors
Abstract: Metabolic flux control analysis of NADH oxidation in bovine heart submitochondrial particles revealed high flux control coefficients for both Complex I and Complex III, suggesting that the two enzymes are functionally associated as a single enzyme, with channelling of the common substrate, Coenzyme Q. This is in contrast with the more accepted view of a mobile diffusable Coenzyme Q pool between these enzymes. Dilution with phospholipids of a mitochondrial fraction enriched in Complexes I and III, with consequent increased theoretical distance between complexes, determines adherence to pool behavior for Coenzyme Q, but only at dilution higher than 1:5 (protein:phospholipids), whereas, at lower phospholipid content, the turnover of NADH cytochrome c reductase is higher than expected by the pool equation.
• Bioblast editor: Komlodi T
Cited by
- Komlódi T, Cardoso LHD, Doerrier C, Moore AL, Rich PR, Gnaiger E (2021) Coupling and pathway control of coenzyme Q redox state and respiration in isolated mitochondria. Bioenerg Commun 2021.3. https://doi.org/10.26124/bec:2021-0003
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MitoFit 2021 CoQ
