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

Latest revision as of 00:03, 23 March 2023

Hatefi Y, Haavik AG, Fowler LR, Griffiths DE (1962) Studies on the electron transfer system XLII. Reconstitution of the electron transfer system. J Biol Chem 237:2661-9. https://doi.org/10.1016/S0021-9258(19)73804-6

» PMID:13905326 Open Access

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

Abstract: 1. It has been shown that the electron transfer system in beef heart mitochondria may be reconstituted either totally or in any desired sequential segment by appropriate combinations of two or more of the four primary complexes that have been isolated in highly purified form in this laboratory.

2. The four enzyme systems that collectively comprise the complete machinery for transfer of electrons from reduced diphosphopyridine nucleotide (DPNH; =NADH) and succinate to oxygen re: I, DPNH-coenzyme Q reductase; II, succinic-coenzyme Q reductase; III, QH2-cytochrome c reductase; and IV, cytochrome c reductase. The specific inhibitors of each complex have been studied.

3. By appropriate combinations of the primary complexes the following secondary activities have been reconstituted: V, DPNH-cytochrome c reductase; VI, succinic-cytochrome c reductase; VII, DPNH, succinic-cytochrome c reductase; VIII, DPNH oxidase; IX, succinic oxidase; and X, DPNH, succinic oxidase activity. The general oxidation-reduction properties of the reconstituted systems, both in the presence and the absence of the usual specific inhibitors of the electron transfer system, are essentially the same as those found for the same activities in the intact mitochondria and in the integrated particles derived therefrom.

4. The reconstituted activities are quite stable to repeated freezing, thawing, and storage at -2O °C, and for the most part, when once formed, are not dissociated by dilution of the mixture or by centrifugation. The evidence supporting the conclusion that reconstitution necessarily involves a particle-particle interaction is discussed. • Keywords: Electron transfer, DPNH-coenzyme Q reductase, Succinic-coenzyme Q reductase, QH2-cytochrome c reductase, Cytochrome c reductase, Beef heart

Electron transfer system versus electron transport chain

More details: »Electron transfer-pathway

Cited by

Gnaiger E (2020) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 5^th ed. Bioenerg Commun 2020.2. https://doi.org/10.26124/bec:2020-0002

Labels:

Organism: Bovines Tissue;cell: Heart Preparation: Isolated mitochondria Enzyme: Complex II;succinate dehydrogenase, Complex IV;cytochrome c oxidase Regulation: Substrate Coupling state: ET

Made history, Electron transfer pathway, BEC 2020.2

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 {{Publication
-|title=Hatefi Y, Haavik AG, Fowler LR, Griffiths DE (1962) Studies on the electron transfer system XLII. Reconstitution of the electron transfer system. J Biol Chem 237: 2661-2669.
+|title=Hatefi Y, Haavik AG, Fowler LR, Griffiths DE (1962) Studies on the electron transfer system XLII. Reconstitution of the electron transfer system. J Biol Chem 237:2661-9. https://doi.org/10.1016/S0021-9258(19)73804-6
 |info=[http://www.jbc.org/content/237/8/2661.full.pdf+html PMID:13905326 Open Access]
 |authors=Hatefi Y, Haavik AG, Fowler LR, Griffiths DE
 |year=1962
 |journal=J Biol Chem
-|abstract=# It  has  been  shown  that  the  electron  transfer  system  in  beef heart  mitochondria  may  be  reconstituted  either  totally  or  in  any desired  sequential  segment  by  appropriate  combinations  of   two or  more  of   the  four  primary  complexes  that  have  been  isolated in  highly  purified  form  in  this  laboratory.
+|abstract=1. It has been shown that the electron transfer system in beef heart mitochondria may be reconstituted either totally or in any desired sequential segment by appropriate combinations of two or more of the four primary  complexes that have been isolated in highly purified form in this laboratory.
-# The  four  enzyme  systems  that  collectively  comprise  the complete  machinery  for  transfer  of   electrons  from  reduced  diphosphopyridine  nucleotide  (DPNH)  and  succinate  to  oxygen re:  I,  DPNH-coenzyme  Q  reductase;  II,  succinic-coenzyme  Q reductase;  III,  QH2-cytochrome  c reductase;  and  IV,  cytochrome c reductase.  The  specific  inhibitors  of   each  complex  have  been studied.
-# By  appropriate  combinations  of   the  primary  complexes  the following  secondary  activities  have  been  reconstituted:  V, DPNH-cytochrome  c  reductase;  VI,  succinic-cytochrome  c  reductase;  VII,  DPNH,  succinic-cytochrome  c  reductase;  VIII, DPNH  oxidase;  IX,  succinic  oxidase;  and  X,  DPNH,  succinic oxidase  activity.  The  general  oxidation-reduction  properties  o f  the  reconstituted  systems,  both  in  the  presence  and  the  absence of  the  usual  specific  inhibitors  of   the  electron  transfer  system,  are essentially  the  same  as  those  found  for  the  same  activities  in  the intact  mitochondria  and  in  the  integrated  particles  derived  therefrom.
-# The  reconstituted  activities  are  quite  stable  to  repeated freezing,  thawing,  and  storage  at  -2O°,  and  for  the  most  part, when  once  formed,  are  not  dissociated  by  dilution  of  the  mixture or  by  centrifugation.  The  evidence  supporting  the  conclusion that  reconstitution  necessarily  involves  a  particle-particle  interaction  is  discussed.
-|keywords=electron transfer, DPNH-coenzyme Q reductase, succinic-coenzyme Q reductase, QH2-cytochrome c reductase, cytochrome c reductase
+. The four enzyme systems that collectively comprise the complete machinery  for transfer of electrons from reduced diphosphopyridine nucleotide (DPNH; =NADH) and succinate to oxygen re: I, DPNH-coenzyme Q reductase; II, succinic-coenzyme Q reductase; III, QH2-cytochrome ''c'' reductase; and IV, cytochrome ''c'' reductase. The specific inhibitors of each complex have been studied.
+. By appropriate combinations of the primary complexes the following secondary activities have been reconstituted: V, DPNH-cytochrome ''c'' reductase;  VI, succinic-cytochrome ''c'' reductase;  VII, DPNH, succinic-cytochrome c reductase; VIII, DPNH oxidase; IX, succinic oxidase; and X, DPNH, succinic oxidase activity. The  general oxidation-reduction properties of the  reconstituted systems, both in the presence and the absence of the usual  specific inhibitors of the electron transfer system, are essentially the same as those found for the same activities in the intact mitochondria and in the  integrated particles derived therefrom.
+. The reconstituted activities are quite stable to repeated freezing, thawing, and storage at -2O °C, and for the most part, when once formed, are not dissociated by dilution of the mixture or by centrifugation. The evidence supporting the conclusion that reconstitution necessarily involves a particle-particle interaction is discussed.
+|keywords=Electron transfer, DPNH-coenzyme Q reductase, Succinic-coenzyme Q reductase, QH2-cytochrome c reductase, Cytochrome c reductase, Beef heart
 }}
+[[File:Hatefi 1962 NS 2012.jpg|right|500px|Q-junction]]
+== Electron transfer system versus electron transport chain ==
+:::* ''More details:'' »[[Electron transfer-pathway]]
+== Cited by ==
+{{Template:Cited by Gnaiger 2020 BEC MitoPathways}}
 {{Labeling
-|organism=Other Mammal
+|organism=Bovines
-|tissues=Cardiac muscle
+|tissues=Heart
-|preparations=Isolated Mitochondria
+|preparations=Isolated mitochondria
-|enzymes=Complex II; Succinate Dehydrogenase, Complex IV; Cytochrome c Oxidase
+|enzymes=Complex II;succinate dehydrogenase, Complex IV;cytochrome c oxidase
-|kinetics=Reduced Substrate; Cytochrome c
+|topics=Substrate
+|couplingstates=ET
+|additional=Made history, Electron transfer pathway, BEC 2020.2
 }}