The cDNA sequences of cytochrome c oxidase subunit VIa from carp and rainbow trout suggest the absence of isoforms in fishes1The sequence data in this paper have been submitted to the GenBank data library under the accession numbers: BankIt88656 U83980 (trout) and BankIt88644 U83907 (carp).1

Hüttemann, Maik; Exner, Stefan; Arnold, Susanne; Lottspeich, Friedrich; Kadenbach, Bernhard

doi:10.1016/s0005-2728(97)00011-x

Cited by 12 publications

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References 12 publications

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“…In fish (trout, carp, and tuna) a third type of subunit VIa was identified, which differs equally from the mammalian isoforms VIaH and VIaL 58, 60. This can be clearly seen in the most parsimonious phylogram of Figure 4, describing the evolutionary relationships between cytochrome c oxidase subunits VIa from different species.…”

Section: High Atp/adp Ratios Decrease the H+/e− Stoichiometry Onlymentioning

confidence: 89%

Cytochrome c Oxidase and the Regulation of Oxidative Phosphorylation

et al. 2001

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Life of higher organisms is essentially dependent on the efficient synthesis of ATP by oxidative phosphorylation in mitochondria. An important and as yet unsolved question of energy metabolism is how are the variable rates of ATP synthesis at maximal work load during exercise or mental work and at rest or during sleep regulated. This article reviews our present knowledge on the structure of bacterial and eukaryotic cytochrome c oxidases and correlates it with recent results on the regulatory functions of nuclear-coded subunits of the eukaryotic enzyme, which are absent from the bacterial enzyme. A new molecular hypothesis on the physiological regulation of oxidative phosphorylation is proposed, assuming a hormonally controlled dynamic equilibrium in vivo between two states of energy metabolism, a relaxed state with low ROS (reactive oxygen species) formation, and an excited state with elevated formation of ROS, which are known to accelerate aging and to cause degenerative diseases and cancer. The hypothesis is based on the allosteric ATP inhibition of cytochrome c oxidase at high intramitochondrial ATP/ADP ratios ("second mechanism of respiratory control"), which is switched on by cAMP-dependent phosphorylation and switched off by calcium-induced dephosphorylation of the enzyme.

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Section: High Atp/adp Ratios Decrease the H+/e− Stoichiometry Onlymentioning

confidence: 89%

Cytochrome c Oxidase and the Regulation of Oxidative Phosphorylation

et al. 2001

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Tissue-Specific Expression of Cytochrome c Oxidase Isoforms and Role in Nonshivering Thermogenesis

Kadenbach

Frank

Linder

et al. 1999

Frontiers of Cellular Bioenergetics

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The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis

Hüttemann¹,

Frank²,

Kadenbach³

1999

CMLS, Cell. Mol. Life Sci.

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A single cDNA of cytochrome c oxidase subunit VIa was characterised from liver, heart and the thermogenic organ of the partially endotherm tuna fish. The amino acid sequence revealed high identity with subunit VIa from carp and trout, but low identity to subunits VIaL (liver type) and VIaH (heart type) of mammalian cytochrome c oxidase. In reconstituted cytochrome c oxidase from bovine heart, the H+/e- stoichiometry is decreased from 1.0 to 0.5 at high intraliposomal ATP/ADP ratios via exchange of bound ADP by ATP at the matrix domain of the transmembraneous subunit VIaH. Reconstituted cytochrome c oxidase from bovine liver and kidney, containing subunit VIaL, revealed H+/e- ratios below 0.5, independent of the ATP/ADP ratio. The results suggest the evolution of three types of subunit VIa. Subunits VIaH and VIaL are postulated to participate in mammalian thermogenesis.

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The cDNA sequences of cytochrome c oxidase subunit VIa from carp and rainbow trout suggest the absence of isoforms in fishes1The sequence data in this paper have been submitted to the GenBank data library under the accession numbers: BankIt88656 U83980 (trout) and BankIt88644 U83907 (carp).1

Cited by 12 publications

References 12 publications

Cytochrome c Oxidase and the Regulation of Oxidative Phosphorylation

Cytochrome c Oxidase and the Regulation of Oxidative Phosphorylation

Tissue-Specific Expression of Cytochrome c Oxidase Isoforms and Role in Nonshivering Thermogenesis

The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis

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