Kinetic advantage of the interaction between the fatty acid β-oxidation enzymes and the complexes of the respiratory chain

B. Sümegi, Zoltan Porpaczy, Istvan Alkonyi

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Respiration-linked oxidation of 3-hydroxybutyryl-CoA, crotonyl-CoA and saturated fatty acyl (C4, C8 and C14)-CoA esters was studied in different mitochondrial preparations. Oxidation of acyl-CoA esters was poor in intact mitochondria; however, it was significant, as well as, NAD+ and CoA-dependent in gently and in vigorously sonicated mitochondria. The respiration-linked oxidation of crotonyl-CoA and 3-hydroxybutyryl-CoA proceeded at much higher rates (over 700%) in gently disrupted mitochondria than in completely disrupted mitochondria. The redox dye-linked oxidation of crotonyl-CoA (with inhibited respiratory chain) was also higher in gently disrupted mitochondria (149%) than in disrupted ones. During the respiration-linked oxidation of 3-hydroxybutyryl-CoA the steady-state NADH concentrations in the reaction chamber were determined, and found to be 8 μM in gently sonicated and 15 μM in completely sonicated mitochondria in spite of the observation that the gently sonicated mitochondria oxidized the 3-hydroxybutyryl-CoA much faster than the completely sonicated mitochondria. The NAD+-dependence of 3-hydroxybutyryl-CoA oxidation showed that a much smaller NAD+ concentration was enough to half-saturate the reaction in gently disrupted mitochondria than in completely disrupted ones. Thus, these observations indicate the positive kinetic consequence of organization of β-oxidation enzyme in situ. Respiration-linked oxidation of bytyryl-, oxtanoyl- and palmitoyl-CoA was also studied and these CoA intermediates were oxidized at approx. 50% of the rate of crotonyl- and 3-hydroxybutyryl-CoA in the gently disrupted mitochondria. In vigorously disrupted mitochondria the oxidation rate of these saturated acyl-CoA intermediates was hardly detectable indicating that the connection between the acyl-CoA dehydrogenase and the respiratory chain had been disrupted.

Original languageEnglish
Pages (from-to)121-128
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume1081
Issue number2
DOIs
Publication statusPublished - Jan 28 1991

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Mitochondria
Electron Transport
Fatty Acids
Oxidation
Kinetics
Enzymes
NAD
Respiration
Coenzyme A
Acyl Coenzyme A
Esters
fatty acid oxidation complex
Acyl-CoA Dehydrogenase
Palmitoyl Coenzyme A
Oxidation-Reduction
3-hydroxybutyryl-coenzyme A
Coloring Agents

Keywords

  • Fatty acid β-oxidation
  • Mitochondrial enzyme
  • Respiratory chain

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Endocrinology

Cite this

Kinetic advantage of the interaction between the fatty acid β-oxidation enzymes and the complexes of the respiratory chain. / Sümegi, B.; Porpaczy, Zoltan; Alkonyi, Istvan.

In: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism, Vol. 1081, No. 2, 28.01.1991, p. 121-128.

Research output: Contribution to journalArticle

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