scholarly journals The Primary Structure of Subunit II of NADH Dehydrogenase from Bovine-Heart Mitochondria

1983 ◽  
Vol 134 (1) ◽  
pp. 145-150 ◽  
Author(s):  
Hedvig BAHR-LINDSTROM ◽  
Yves M. GALANTE ◽  
Magnus PERSSON ◽  
Hans JORNVALL
Keyword(s):  
Primary Structure ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
Bovine Heart

scholarly journals THE PRIMARY STRUCTURE OF SUBUNIT II OF NADH DEHYDROGENASE FROM BOVINE-HEART MITOCHONDRIA

1983 ◽  
Vol 134 (1) ◽  
pp. 149-150
Author(s):  
Hedvig Bahr-Lindstrom ◽  
Yves M. Galante ◽  
Magnus Persson ◽  
Hans Jornvall
Keyword(s):  
Primary Structure ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
Bovine Heart

Kinetic of Superoxide Formation by Respiratory Chain NADH-Dehydrogenase of Bovine Heart Mitochondria

1983 ◽  
Vol 94 (4) ◽  
pp. 1301-1306 ◽  
Author(s):  
Dongchon KANG ◽  
Hideki NARABAYASHI ◽  
Takeyoshi SATA ◽  
koichiro TAKESHIGE
Keyword(s):  
Respiratory Chain ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
Bovine Heart ◽  
Superoxide Formation

scholarly journals Purification and Characteristics of a Butyryl Coenzyme A Synthetase from Bovine Heart Mitochondria

1965 ◽  
Vol 240 (1) ◽  
pp. 29-33
Author(s):  
Leslie T. Webster ◽  
Lance D. Gerowin ◽  
Louis Rakita
Keyword(s):  
Coenzyme A ◽  
Heart Mitochondria ◽  
Bovine Heart

scholarly journals ATP Synthase Complex from Bovine Heart Mitochondria

1989 ◽  
Vol 264 (26) ◽  
pp. 15548-15551
Author(s):  
S Joshi ◽  
M J Pringle
Keyword(s):  
Atp Synthase ◽  
Heart Mitochondria ◽  
Bovine Heart

scholarly journals Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria

1980 ◽  
Vol 191 (2) ◽  
pp. 421-427 ◽  
Author(s):  
J F Turrens ◽  
A Boveris
Keyword(s):  
Cytochrome B ◽  
Nadh Dehydrogenase ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Biphasic Effect ◽  
Carbonyl Cyanide ◽  
Autocatalytic Process ◽  
Ph Range ◽  
Energy Dependent ◽  
O2 Production

Submitochondrial particles from bovine heart in which NADH dehydrogenase is reduced by either addition of NADH and rotenone or by reversed electron transfer generate 0.9 +/- 0.1 nmol of O2-/min per mg of protein at pH 7.4 and at 30 degrees C. When NADH is used as substrate, rotenone, antimycin and cyanide increase O2- production. In NADH- and antimycin-supplemented submitochondrial particles, rotenone has a biphasic effect: it increases O2- production at the NADH dehydrogenase and it inhibits O2- production at the ubiquinone-cytochrome b site. The generation of O2- by the rotenone, the uncoupler carbonyl cyanide rho-trifluoromethoxyphenylhydrazone and oligomycin at concentrations similar to those required to inhibit energy-dependent succinate-NAD reductase. Cyanide did not affect O2- generation at the NADH dehydrogenase, but inhibited O2- production at the ubiquinone-cytochrome b site. Production of O2- at the NADH dehydrogenase is about 50% of the O2- generation but the ubiquinone-cytochrome b area at pH 7.4. Additivity of the two mitochondrial sites of O2- generation was observed over the pH range from 7.0 to 8.8. AN O2–dependent autocatalytic process that requires NADH, submitochondrial particles and adrenaline is described.

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