Difference between revisions of "Hatefi 1962 J Biol Chem-XLI"

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Hatefi Y, Haavik AG, Griffiths DE (1962) Studies on the electron transfer system XLI. Reduced coenzyme Q (QH2)-cytochrome c reductase. J Biol Chem 237: 1681-1685.

» PMID: 13905328; Open Access

Hatefi Y, Haavik AG, Griffiths DE (1962) J Biol Chem

Abstract: The preparation from beef heart mitochondria and the properties, of a highly active and stable enzyme system, capable of catalyzing the reduction of cytochrome c by reduced coenzyme Q2 are described. The enzyme complex contains cytochrome b and cytochrome c1 in high concentration, and is free of cytochrome c oxidase, cytochrome c, flavoproteins, and the citric acid cycle dehydrogenases. The activity of the enzyme corresponds to a QO2, of about 320,000 at 38°. This activity is strongly inhibited by antimycin A, 2-nonyl-4-hydroxy-quinoline-N-oxide, and 2-alkyl-3-hydroxynaphthoquinone. Amytal, thenoyltrifluoroacetone, and a number of specific metal-chelating compounds are ineffective as inhibitors. • Keywords: coenzyme Q, reduced coenzyme Q (QH2), cytochrome c reductase

Labels:

Organism: Other Mammal"Other Mammal" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property. Tissue;cell: Cardiac muscle"Cardiac muscle" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property. Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property. Enzyme: Complex IV; Cytochrome c Oxidase"Complex IV; Cytochrome c Oxidase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.

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 {{Publication
 |title=Hatefi Y, Haavik AG, Griffiths DE (1962) Studies on the electron transfer system XLI. Reduced coenzyme Q (QH2)-cytochrome c reductase. J Biol Chem 237: 1681-1685.
 |info=[http://www.ncbi.nlm.nih.gov/pubmed/13905328 PMID: 13905328]; [http://www.jbc.org/content/237/5/1681.full.pdf+html Open Access]
 |authors=Hatefi Y, Haavik AG, Griffiths DE
 |year=1962
 |journal=J Biol Chem
-|abstract=The  preparation  from  beef  heart  mitochondria  and  the  properties,  o f   a  highly  active  and  stable  enzyme  system,  capable  of  catalyzing  the  reduction  of   cytochrome  c by  reduced  coenzyme  Q2 are  described.  The  enzyme  complex  contains  cytochrome  b and cytochrome  c1 in  high  concentration,  and  is  free  of   cytochrome  c oxidase,  cytochrome  c,  flavoproteins,  and  the  citric  acid  cycle dehydrogenases.  The  activity  of   the  enzyme  corresponds  to  a QO2,  of   about  320,000  at  38°.  This  activity  is  strongly  inhibited by  antimycin  A,  2-nonyl-4-hydroxy-quinoline-N-oxide,  and 2-alkyl-3-hydroxynaphthoquinone.  Amytal,  thenoyltrifluoroacetone,  and a number  of   specific  metal-chelating  compounds  are ineffective  as  inhibitors.
+|abstract=The  preparation  from  beef  heart  mitochondria  and  the  properties,  of   a  highly  active  and  stable  enzyme  system,  capable  of  catalyzing  the  reduction  of   cytochrome  c by  reduced  coenzyme  Q2 are  described.  The  enzyme  complex  contains  cytochrome  b and cytochrome  c1 in  high  concentration,  and  is  free  of   cytochrome  c oxidase,  cytochrome  c,  flavoproteins,  and  the  citric  acid  cycle dehydrogenases.  The  activity  of   the  enzyme  corresponds  to  a QO2,  of   about  320,000  at  38°.  This  activity  is  strongly  inhibited by  antimycin  A,  2-nonyl-4-hydroxy-quinoline-N-oxide,  and 2-alkyl-3-hydroxynaphthoquinone.  Amytal,  thenoyltrifluoroacetone,  and a number  of   specific  metal-chelating  compounds  are ineffective  as  inhibitors.
 |keywords=coenzyme Q, reduced coenzyme Q (QH2), cytochrome c reductase
 }}