Bernhard Kadenbach
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Bernhard Kadenbach has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
Susanne Arnold
Zelluläre Neurowissenschaften, Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany
4 shared publications- Maik Hüttemann
Center for Molecular Medicine and Genetics Wayne State University Detroit Michigan USA
3 shared publications Icksoo Lee
Molecular Medicine and Genetics, Wayne State University, School of Medicine, Detroit, MI 48201, USA
2 shared publicationsElisabeth Bender
1 shared publicationKara Follmann
Fachbereich Chemie, Philipps-Universität, Marburg, Germany
1 shared publicationShelagh Ferguson‐Miller
Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824, USA
1 shared publication
Latest Publications
- 1 April 2004
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 1655, 400-408
The possible role of cytochrome c oxidase in stress-induced apoptosis and degenerative diseases
- 1 April 2004
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 1655, 400-408
The possible role of cytochrome c oxidase in stress-induced apoptosis and degenerative diseases
- 1 June 2003
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 1604 (2) , 77-94
Intrinsic and extrinsic uncoupling of oxidative phosphorylation
- 1 June 2003
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 1604 (2) , 77-94
Intrinsic and extrinsic uncoupling of oxidative phosphorylation
- 1 August 2000
- Published by Elsevier in Free Radical Biology and Medicine
- Vol. 29 (3-4) , 211-221
Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase11This article is dedicated to the memory of the late Professor Lars Ernster.
- 1 August 2000
- Published by Elsevier in Free Radical Biology and Medicine
- Vol. 29 (3-4) , 211-221
Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase11This article is dedicated to the memory of the late Professor Lars Ernster.
- 1 August 1999
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 55 (11) , 1482-1490
The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis
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.
- 1 August 1999
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 55 (11) , 1482-1490
The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis
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.
- 26 March 1999
- Published by Wiley in FEBS Letters
- Vol. 447 (2-3) , 131-134
A second mechanism of respiratory control
According to the chemosmotic hypothesis, ATP is synthesized in mitochondria, bacteria and chloroplasts via the proton motive force Δp, the energy‐rich intermediate of electron transport and photosynthetic phosphorylation. The general applicability of the chemosmotic hypothesis, however, was disputed until present. In particular the relationship between the rate of respiration and Δp in mitochondria was found variable, depending on the experimental conditions. Recently, a new mechanism of respiratory control was found, based on binding of ATP or ADP to subunit IV of cytochrome c oxidase, which is independent of Δp and could explain many previous results contradicting the chemosmotic hypothesis.
- 26 March 1999
- Published by Wiley in FEBS Letters
- Vol. 447 (2-3) , 131-134
A second mechanism of respiratory control
According to the chemosmotic hypothesis, ATP is synthesized in mitochondria, bacteria and chloroplasts via the proton motive force Δp, the energy‐rich intermediate of electron transport and photosynthetic phosphorylation. The general applicability of the chemosmotic hypothesis, however, was disputed until present. In particular the relationship between the rate of respiration and Δp in mitochondria was found variable, depending on the experimental conditions. Recently, a new mechanism of respiratory control was found, based on binding of ATP or ADP to subunit IV of cytochrome c oxidase, which is independent of Δp and could explain many previous results contradicting the chemosmotic hypothesis.
- Open Access
- 1 August 1998
- Published by Wiley in IUBMB Life
- Vol. 45 (5) , 1047-1055
Cytochrome C oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP
The activity of reconstituted cytochrome c oxidase from bovine heart but not from Rhodobacter sphaeroides is allosterically inhibited by intraliposomal ATP, which binds to subunit IV. The activity of cytochrome c oxidase of wild-type yeast and of a subunit VIa-deleted yeast mutant, measured with Tween 20-solubilized mitochondria in the presence of an ATP-regenerating system, was also allosterically inhibited by ATP, indicating the general validity of this mechanism of “respiratory control” in eucaryotic cytochrome c oxidases (Arnold and Kadenbach, Eur. J. Biochem. (1997) 249, 350–354). Deletion of subunit Via changes the biphysic into monophysic kinetics of the yeast enzyme in the presence of ADP. A tenfold higher amount of horse heart cytochrome c, as compared to yeast cytochrome c, was required to relieve the ATP inhibition of the yeast enzyme.
- 1 August 1998
- Published by Wiley in IUBMB Life
- Vol. 45 (5) , 1047-1055
Open AccessCytochrome C oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP
The activity of reconstituted cytochrome c oxidase from bovine heart but not from Rhodobacter sphaeroides is allosterically inhibited by intraliposomal ATP, which binds to subunit IV. The activity of cytochrome c oxidase of wild-type yeast and of a subunit VIa-deleted yeast mutant, measured with Tween 20-solubilized mitochondria in the presence of an ATP-regenerating system, was also allosterically inhibited by ATP, indicating the general validity of this mechanism of “respiratory control” in eucaryotic cytochrome c oxidases (Arnold and Kadenbach, Eur. J. Biochem. (1997) 249, 350–354). Deletion of subunit Via changes the biphysic into monophysic kinetics of the yeast enzyme in the presence of ADP. A tenfold higher amount of horse heart cytochrome c, as compared to yeast cytochrome c, was required to relieve the ATP inhibition of the yeast enzyme.