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Difference between revisions of "Chance 1961 J Biol Chem-IV"

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{{Publication
{{Publication
|title=Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria IV. The pathway of electron transfer. J Biol Chem 236: 1562-1568.  
|title=Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria IV. The pathway of electron transfer. J Biol Chem 236:1562-8.
|info=[http://www.jbc.org/content/236/5/1562.full.pdf+html PMID: 13692279 Open Access]
|info=[http://www.jbc.org/content/236/5/1562.full.pdf+html PMID: 13692279 Open Access]
|authors=Chance B, Hollunger G
|authors=Chance B, Hollunger G
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# Three  mechanisms  for  increased  reduction  of  pyridine nucleotide  in  succinate-treated  mitochondria  that  do  not  involve the  above  pathway  fail  to  show  responses  of  the  experimentally observed  sensitivity  to  Amytal  or  to  antimycin  A.  
# Three  mechanisms  for  increased  reduction  of  pyridine nucleotide  in  succinate-treated  mitochondria  that  do  not  involve the  above  pathway  fail  to  show  responses  of  the  experimentally observed  sensitivity  to  Amytal  or  to  antimycin  A.  
# The  properties  of  the  energy-linked  pool  of  pyridine  nucleotide  in  metabolism  are  considered. Its  participation  is  likely  to be  small  in  state  3 and  of  some  consequence  in  state  4.
# The  properties  of  the  energy-linked  pool  of  pyridine  nucleotide  in  metabolism  are  considered. Its  participation  is  likely  to be  small  in  state  3 and  of  some  consequence  in  state  4.
|keywords=electron transfer, succinate, pyridine nucleotide, antimycin A
|keywords=Electron transfer, Succinate, Pyridine nucleotide, Antimycin A
}}
}}
{{Labeling
{{Labeling
|organism=Other Mammal, Other Non-Mammal
|organism=Guinea pig, Birds
|tissues=Cardiac muscle, Hepatocyte; Liver, Kidney
|tissues=Heart, Liver, Kidney
|preparations=Isolated Mitochondria
|preparations=Isolated mitochondria
|enzymes=Complex II; Succinate Dehydrogenase
|enzymes=Complex II;succinate dehydrogenase, Complex III
|topics=Respiration; OXPHOS; ETS Capacity
|couplingstates=OXPHOS
|additional=Made history
|additional=Made history
}}
}}

Latest revision as of 09:54, 9 November 2016

Publications in the MiPMap
Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria IV. The pathway of electron transfer. J Biol Chem 236:1562-8.

» PMID: 13692279 Open Access

Chance B, Hollunger G (1961) J Biol Chem

Abstract:

  1. The pathway of electron transfer from succinate to pyridine nucleotide shows a sensitivity to antimycin A, suggesting that carriers of the respiratory chain up to and including the antimycin-sensitive point are involved in succinate-linked reduction of pyridine nucleotide.
  2. The sensitivity of succinate-linked reduction of pyridine nucleotide to Amytal suggests that a reverse of the flavoprotein-pyridine nucleotide interaction observed in the oxidation of pyridine nucleotide in phosphorylating mitochondria is also part of the electron transfer pathway.
  3. Mechanisms indicating the interconnection of electrons from the antimycin-sensitive point to this flavoprotein via electron carriers such as cytochrome b and ubiquinone are considered. These mechanisms appear to apply to both aerobic and anaerobic (terminally inhibited) energy-linked reduction of pyridine nucleotide.
  4. Three mechanisms for increased reduction of pyridine nucleotide in succinate-treated mitochondria that do not involve the above pathway fail to show responses of the experimentally observed sensitivity to Amytal or to antimycin A.
  5. The properties of the energy-linked pool of pyridine nucleotide in metabolism are considered. Its participation is likely to be small in state 3 and of some consequence in state 4.

Keywords: Electron transfer, Succinate, Pyridine nucleotide, Antimycin A


Labels:


Organism: Guinea pig, Birds  Tissue;cell: Heart, Liver, Kidney  Preparation: Isolated mitochondria  Enzyme: Complex II;succinate dehydrogenase, Complex III 

Coupling state: OXPHOS 


Made history