ATP Synthesis by Purified ATP-Synthase from Beef Heart Mitochondria After Coreconstitution with Bacteriorhodopsin

1995 ◽  
Vol 322 (1) ◽  
pp. 135-142 ◽  
Author(s):  
S. Matuschka ◽  
K. Zwicker ◽  
T. Nawroth ◽  
G. Zimmer
Keyword(s):  
Atp Synthase ◽  
Atp Synthesis ◽  
Heart Mitochondria ◽  
Beef Heart ◽  
Beef Heart Mitochondria

scholarly journals Proteomic Analysis of Peroxynitrite-Induced Protein Nitration in Isolated Beef Heart Mitochondria

2018 ◽  
pp. 239-250 ◽  
Author(s):  
M. KOHUTIAR ◽  
A. ECKHARDT ◽  
I. MIKŠÍK ◽  
P. ŠANTOROVÁ ◽  
J. WILHELM
Keyword(s):  
Atp Synthase ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
2D Electrophoresis ◽  
Beef Heart ◽  
Protein Nitration ◽  
Iron Sulfur ◽  
Beef Heart Mitochondria ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

Mitochondria are exposed to reactive nitrogen species under physiological conditions and even more under several pathologic states. In order to reveal the mechanism of these processes we studied the effects of peroxynitrite on isolated beef heart mitochondria in vitro. Peroxynitrite has the potential to nitrate protein tyrosine moieties, break the peptide bond, and eventually release the membrane proteins into the solution. All these effects were found in our experiments. Mitochondrial proteins were resolved by 2D electrophoresis and the protein nitration was detected by immunochemical methods and by nano LC-MS/MS. Mass spectrometry confirmed nitration of ATP synthase subunit beta, pyruvate dehydrogenase E1 component subunit beta, citrate synthase and acetyl-CoA acetyltransferase. Immunoblot detection using chemiluminiscence showed possible nitration of other proteins such as cytochrome b-c1 complex subunit 1, NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, elongation factor Tu, NADH dehydrogenase [ubiquinone] flavoprotein 2, heat shock protein beta-1 and NADH dehydrogenase [ubiquinone] iron-sulfur protein 8. ATP synthase beta subunit was nitrated both in membrane and in fraction prepared by osmotic lysis. The high sensitivity of proteins to nitration by peroxynitrite is of potential biological importance, as these enzymes are involved in various pathways associated with energy production in the heart.

scholarly journals Structure of the ATP-Synthase from Chloroplasts and Mitochondria Studied by Electron Microscopy

1988 ◽  
Vol 43 (3-4) ◽  
pp. 219-225 ◽  
Author(s):  
Egbert J. Boekema ◽  
Günter Schmidt ◽  
Peter Gräber ◽  
Jan A. Berden
Keyword(s):  
Electron Microscopy ◽  
Atp Synthase ◽  
Heart Mitochondria ◽  
Cylindrical Shape ◽  
Beef Heart ◽  
Mitochondrial Enzyme ◽  
Spinach Chloroplasts ◽  
Beef Heart Mitochondria

The structure of the ATP-synthase, F0F1, from spinach chloroplasts and beef heart mitochondria has been investigated by electron microscopy with negatively stained specimens. The detergent- solubilized ATP-synthase forms string-like structures in which the F0 parts are aggregated. In most cases, the F1 parts are arranged at alternating sides along the string. The F0 part has an approximate cylindrical shape with heights of 8.3 and 8.9 nm and diameters of 6.2 and 6.4 nm for the chloroplast and mitochondrial enzyme, respectively. The F1 parts are disk-like structures with a diameter of about 11.5 nm and a height of about 8.5 nm. The F, parts are attached to the strings, composed of F0 parts, in most cases, with their smallest dimension parallel to the strings. The stalk connecting F0 and F1 has a length of 3.7 nm and 4.3 nm and a diameter of 2.7 nm and 4.3 nm for the chloroplast and mitochondrial enzyme, respectively.

scholarly journals Proteomic Analysis of Peroxynitrite-Induced Protein Nitration in Isolated Beef Heart Mitochondria

2018 ◽  
pp. 239-250 ◽  
Author(s):  
M. KOHUTIAR ◽  
A. ECKHARDT ◽  
I. MIKŠÍK ◽  
P. ŠANTOROVÁ ◽  
J. WILHELM
Keyword(s):  
Atp Synthase ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
2D Electrophoresis ◽  
Beef Heart ◽  
Protein Nitration ◽  
Iron Sulfur ◽  
Beef Heart Mitochondria ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

Mitochondria are exposed to reactive nitrogen species under physiological conditions and even more under several pathologic states. In order to reveal the mechanism of these processes we studied the effects of peroxynitrite on isolated beef heart mitochondria in vitro. Peroxynitrite has the potential to nitrate protein tyrosine moieties, break the peptide bond, and eventually release the membrane proteins into the solution. All these effects were found in our experiments. Mitochondrial proteins were resolved by 2D electrophoresis and the protein nitration was detected by immunochemical methods and by nano LC-MS/MS. Mass spectrometry confirmed nitration of ATP synthase subunit beta, pyruvate dehydrogenase E1 component subunit beta, citrate synthase and acetyl-CoA acetyltransferase. Immunoblot detection using chemiluminiscence showed possible nitration of other proteins such as cytochrome b-c1 complex subunit 1, NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, elongation factor Tu, NADH dehydrogenase [ubiquinone] flavoprotein 2, heat shock protein beta-1 and NADH dehydrogenase [ubiquinone] iron-sulfur protein 8. ATP synthase beta subunit was nitrated both in membrane and in fraction prepared by osmotic lysis. The high sensitivity of proteins to nitration by peroxynitrite is of potential biological importance, as these enzymes are involved in various pathways associated with energy production in the heart.

scholarly journals Tetrachlorohydroquinone Oxidase Activity in Beef Heart Mitochondria

1965 ◽  
Vol 240 (4) ◽  
pp. 1788-1795 ◽  
Author(s):  
Joseph M. Machinist ◽  
F.L. Crane ◽  
Earl E. Jacobs
Keyword(s):  
Oxidase Activity ◽  
Heart Mitochondria ◽  
Beef Heart ◽  
Beef Heart Mitochondria
Sign in / Sign up

Export Citation Format

Share Document