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Cytochrome C oxidase and the regulation of oxidative phosphorylation.
Ludwig B, Bender E, Arnold S, Hüttemann M, Lee I, Kadenbach B. Ludwig B, et al. Chembiochem. 2001 Jun 1;2(6):392-403. doi: 10.1002/1439-7633(20010601)2:6<392::AID-CBIC392>3.0.CO;2-N. Chembiochem. 2001. PMID: 11828469 Review.
Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase.
Kadenbach B, Hüttemann M, Arnold S, Lee I, Bender E. Kadenbach B, et al. Free Radic Biol Med. 2000 Aug;29(3-4):211-21. doi: 10.1016/s0891-5849(00)00305-1. Free Radic Biol Med. 2000. PMID: 11035249 Review.
High substrate pressure (sigmoidal v/s kinetics), palmitate and 3,5-diiodothyronine (binding to subunit Va) increase also delta p, ROS production and slip but without dephosphorylation of COX....
High substrate pressure (sigmoidal v/s kinetics), palmitate and 3,5-diiodothyronine (binding to subunit Va) increase also delta p, RO …
Turkey cytochrome c oxidase contains subunit VIa of the liver type associated with low efficiency of energy transduction.
Hüttemann M, Arnold S, Lee I, Mühlenbein N, Linder D, Lottspeich F, Kadenbach B. Hüttemann M, et al. Eur J Biochem. 2000 Apr;267(7):2098-104. doi: 10.1046/j.1432-1327.2000.01216.x. Eur J Biochem. 2000. PMID: 10727950
A second mechanism of respiratory control.
Kadenbach B, Arnold S. Kadenbach B, et al. FEBS Lett. 1999 Mar 26;447(2-3):131-4. doi: 10.1016/s0014-5793(99)00229-x. FEBS Lett. 1999. PMID: 10214932 Review.
Cytochrome c oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP.
Follmann K, Arnold S, Ferguson-Miller S, Kadenbach B. Follmann K, et al. Biochem Mol Biol Int. 1998 Aug;45(5):1047-55. doi: 10.1002/iub.7510450522. Biochem Mol Biol Int. 1998. PMID: 9739469
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 mech …
The activity of cytochrome c oxidase of wild-type yeast and of a subunit VIa-deleted yeast mutant, measured with Tween 20-solubilized mitoch …
3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP.
Arnold S, Goglia F, Kadenbach B. Arnold S, et al. Eur J Biochem. 1998 Mar 1;252(2):325-30. doi: 10.1046/j.1432-1327.1998.2520325.x. Eur J Biochem. 1998. PMID: 9523704
We demonstrate specific binding of labelled 3,5-diiodothyronine to subunit Va of cytochrome-c oxidase from bovine heart. 3,5-Diiodothyronine, and to a small extent triiodothyronine, but not thyroxine and thyronine, abolish the allosteric inhibition of ascorbate respiration of rec …
We demonstrate specific binding of labelled 3,5-diiodothyronine to subunit Va of cytochrome-c oxidase from bovine heart. 3,5-Diiodothyronine …
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