scholarly journals Inhibitory Effect of NaCl on Hog Kidney Mitochondrial Membrane-Bound Monoamine Oxidase: pH and Temperature Dependences

1995 ◽  
Vol 69 (4) ◽  
pp. 293-302 ◽  
Author(s):  
Yoko Omura
Keyword(s):  
Monoamine Oxidase ◽  
Mitochondrial Membrane ◽  
Inhibitory Effect ◽  
Temperature Dependences ◽  
Membrane Bound ◽  
Hog Kidney

MITOCHONDRIAL MEMBRANE-BOUND STEROID HYDROXYLATING SYSTEMS: STRUCTURE AND FUNCTIONS

1980 ◽  
pp. 131-134
Author(s):  
A.A. Akhrem ◽  
V.N. Lapko ◽  
A.G. Lapko ◽  
S.P. Martsev ◽  
V.M. Shkumatov ◽  
...  
Keyword(s):  
Mitochondrial Membrane ◽  
Membrane Bound ◽  
Structure And Functions

scholarly journals Effects of 2-mercaptoacetate in isolated liver mitochondria in vitro. Competitive inhibition of 3-hydroxybutyrate dehydrogenase and depression of the β-oxidation pathway

1982 ◽  
Vol 206 (1) ◽  
pp. 53-59 ◽  
Author(s):  
F Bauché ◽  
D Sabourault ◽  
Y Giudicelli ◽  
J Nordmann ◽  
R Nordmann
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Competitive Inhibition ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Acid Oxidation ◽  
Membrane Bound ◽  
Energy Dependent ◽  
Isolated Liver

The effects of 2-mercaptoacetate on the respiration rates induced by different substrates were studied in vitro in isolated liver mitochondria. With palmitoyl-L-carnitine or 2-oxoglutarate as the substrate, the ADP-stimulated respiration (State 3) was dose-dependently inhibited by 2-mercaptoacetate. with glutamate or succinate as the substrate. State-3 respiration was only slightly inhibited by 2-mercaptoacetate. In contrast, the oxidation rate of 3-hydroxybutyrate was competitively inhibited by 2-mercaptoacetate in both isolated mitochondria and submitochondrial particles. In uncoupled mitochondria and in mitochondria in which ATP- and GTP-dependent acyl-CoA biosynthesis was inhibited, the inhibitory effect of 2-mercaptoacetate on palmitoyl-L-carnitine oxidation was abolished; under the same conditions, however, inhibition of 3-hydroxybutyrate oxidation by 2-mercaptoacetate still persisted. These results led to the following conclusions: 2-mercaptoacetate itself enters the mitochondrial matrix, inhibits fatty acid oxidation through a mechanism requiring an energy-dependent activation of 2-mercaptoacetate and itself inhibits 3-hydroxybutyrate oxidation through a competitive inhibition of the membrane-bound 3-hydroxybutyrate dehydrogenase. This study also strongly suggests that the compound responsible for the inhibition of fatty acid oxidation is 2-mercaptoacetyl-CoA.

scholarly journals Molecular mechanism of mitochondrial phosphatidate transfer by Ups1

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Jiuwei Lu ◽  
Chun Chan ◽  
Leiye Yu ◽  
Jun Fan ◽  
Fei Sun ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Mitochondrial Membrane ◽  
Outer Mitochondrial Membrane ◽  
Mitochondrial Membranes ◽  
Inner Mitochondrial Membrane ◽  
Membrane Interaction ◽  
Detailed Mechanism ◽  
Physiological Regulator ◽  
Membrane Bound ◽  
Dynamics Simulations

AbstractCardiolipin, an essential mitochondrial physiological regulator, is synthesized from phosphatidic acid (PA) in the inner mitochondrial membrane (IMM). PA is synthesized in the endoplasmic reticulum and transferred to the IMM via the outer mitochondrial membrane (OMM) under mediation by the Ups1/Mdm35 protein family. Despite the availability of numerous crystal structures, the detailed mechanism underlying PA transfer between mitochondrial membranes remains unclear. Here, a model of Ups1/Mdm35-membrane interaction is established using combined crystallographic data, all-atom molecular dynamics simulations, extensive structural comparisons, and biophysical assays. The α2-loop, L2-loop, and α3 helix of Ups1 mediate membrane interactions. Moreover, non-complexed Ups1 on membranes is found to be a key transition state for PA transfer. The membrane-bound non-complexed Ups1/ membrane-bound Ups1 ratio, which can be regulated by environmental pH, is inversely correlated with the PA transfer activity of Ups1/Mdm35. These results demonstrate a new model of the fine conformational changes of Ups1/Mdm35 during PA transfer.

Tween-20 Activates and Solubilizes the Mitochondrial Membrane-bound, Calmodulin Dependent NAD + Kinase of Avena sativa L.

2001 ◽  
Vol 182 (2) ◽  
pp. 135-146 ◽  
Author(s):  
M.-A. Pou de Crescenzo ◽  
S. Gallais ◽  
A. Léon ◽  
D.L. Laval-Martin
Keyword(s):  
Avena Sativa ◽  
Mitochondrial Membrane ◽  
Tween 20 ◽  
Nad Kinase ◽  
Membrane Bound
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