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Difference between revisions of "Singer 1956 J Biol Chem"

From Bioblast
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# Among  the  common  electron  acceptors,  only  the  following  function with  the  dehydrogenase,  at  the  relative  rates  indicated  in  parentheses: phenazine  methosulfate  (100),  ferricyanide  (39),  O2 (0.02).  The  first  two of  these  acceptors  react  via  the  iron  moieties,  whereas  O2  seems  to  react directly  with  the  flavin.  
# Among  the  common  electron  acceptors,  only  the  following  function with  the  dehydrogenase,  at  the  relative  rates  indicated  in  parentheses: phenazine  methosulfate  (100),  ferricyanide  (39),  O2 (0.02).  The  first  two of  these  acceptors  react  via  the  iron  moieties,  whereas  O2  seems  to  react directly  with  the  flavin.  
# The  QO2,  has  been  measured  as  20,000 and  the  turnover  number  as 3000  under  the  standard  assay  conditions.  
# The  QO2,  has  been  measured  as  20,000 and  the  turnover  number  as 3000  under  the  standard  assay  conditions.  
# The  properties  of  the  isolated  dehydrogenase  agree  with  those  previously  described  for  mitochondrial  and  other  particulate  preparations  of the  enzyme,  except  for  properties  related  to  the  absence  of  contaminating hemoproteins.  At  38° the  pH  optimum  is  7.7;  the  K,  for  succinate  is 1.3  X  10-3 M  at  38° and  5.2  X  10-4 M  at  21°.  Oxalacetate,  malonate,  and fumarate  are  competitive  inhibitors.  Antimycin  A  and  BAL  do  not  inhibit  the  dehydrogenase.  The  dehydrogenase  is  highly  sensitive  to  sulfhydryl  reagents,  p-chloromercuribenzoate  inhibiting  it  in  a  reversible  manner  and  the  substrate  protecting  the  enzyme  from  this  type  of  inhibition.
# The  properties  of  the  isolated  dehydrogenase  agree  with  those  previously  described  for  mitochondrial  and  other  particulate  preparations  of the  enzyme,  except  for  properties  related  to  the  absence  of  contaminating hemoproteins.  At  38 °C the  pH  optimum  is  7.7;  the  K,  for  succinate  is 1.3  X  10-3 M  at  38 °C and  5.2  X  10-4 M  at  21 °C.  Oxalacetate,  malonate,  and fumarate  are  competitive  inhibitors.  Antimycin  A  and  BAL  do  not  inhibit  the  dehydrogenase.  The  dehydrogenase  is  highly  sensitive  to  sulfhydryl  reagents,  p-chloromercuribenzoate  inhibiting  it  in  a  reversible  manner  and  the  substrate  protecting  the  enzyme  from  this  type  of  inhibition.
|keywords=Succinic dehydrogenase, Beef heart mitochondria
|keywords=Succinic dehydrogenase, Beef heart mitochondria
}}
}}
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|organism=Bovines
|organism=Bovines
|tissues=Heart
|tissues=Heart
|preparations=Isolated Mitochondria
|preparations=Isolated Mitochondria, SMP
|enzymes=Complex II; Succinate Dehydrogenase
|enzymes=Complex II; Succinate Dehydrogenase
|kinetics=Oxygen
|topics=Inhibitor kinetics, Temperature
|additional=Made history
|additional=Made history
}}
}}

Revision as of 09:09, 11 August 2013

Publications in the MiPMap
Singer TP, Kearney, EB and Bernath P (1956) Studies on succinic dehydrogenase. Isolation and properties of the dehydrogenase from beef heart. J Biol Chem 223: 599-613.

» PMID: 13385208 Open Access

Singer TP, Kearney, EB and Bernath P (1956) J Biol Chem

Abstract:

  1. Succinic dehydrogenase has been isolated from beef heart mitochondria as a soluble protein in a state approaching homogeneity by physico-chemical criteria. The overall purification is about 100-fold compared with a mitochondrial acetone powder.
  2. The enzyme is a ferroflavoprotein cont,aining 4 atoms of ferrous (non-hemin) iron and a mole of flavin per mole of protein (200,000 gm.). The dehydrogenase may be isolated from aged starting material with 2 atoms of iron per mole and half the specific activity.
  3. Among the common electron acceptors, only the following function with the dehydrogenase, at the relative rates indicated in parentheses: phenazine methosulfate (100), ferricyanide (39), O2 (0.02). The first two of these acceptors react via the iron moieties, whereas O2 seems to react directly with the flavin.
  4. The QO2, has been measured as 20,000 and the turnover number as 3000 under the standard assay conditions.
  5. The properties of the isolated dehydrogenase agree with those previously described for mitochondrial and other particulate preparations of the enzyme, except for properties related to the absence of contaminating hemoproteins. At 38 °C the pH optimum is 7.7; the K, for succinate is 1.3 X 10-3 M at 38 °C and 5.2 X 10-4 M at 21 °C. Oxalacetate, malonate, and fumarate are competitive inhibitors. Antimycin A and BAL do not inhibit the dehydrogenase. The dehydrogenase is highly sensitive to sulfhydryl reagents, p-chloromercuribenzoate inhibiting it in a reversible manner and the substrate protecting the enzyme from this type of inhibition.

Keywords: Succinic dehydrogenase, Beef heart mitochondria


Labels:


Organism: Bovines  Tissue;cell: Heart  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., SMP  Enzyme: Complex II; Succinate Dehydrogenase"Complex II; Succinate Dehydrogenase" 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.  Regulation: Inhibitor kinetics"Inhibitor kinetics" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property., Temperature 



Made history