Related Experiment Video

Updated: Jan 3, 2026

Model of Ischemia and Reperfusion Injury in Rabbits
06:11

Model of Ischemia and Reperfusion Injury in Rabbits

Published on: November 3, 2023

1.7K

Brain Ischemia/Reperfusion Injury and Mitochondrial Complex I Damage

A Galkin1

  • 1Division of Neonatology, Department of Pediatrics, Columbia University William Black Building, NY 10032, New York, USA. ag4003@cumc.columbia.edu.

Biochemistry. Biokhimiia
|November 26, 2019
PubMed

Insights

Brain mitochondria complex I is vulnerable to ischemia/reperfusion (I/R) injury. Recent studies reveal two key damage mechanisms: cofactor dissociation and critical cysteine modification, impacting brain energy failure.

Area of Science:

  • Neuroscience
  • Mitochondrial Biology
  • Biochemistry

Background:

  • Ischemic stroke and neonatal hypoxic-ischemic encephalopathy are leading causes of disability.
  • Brain energy metabolism relies on mitochondrial oxidative phosphorylation.
  • Ischemia/reperfusion (I/R) disrupts ATP production, causing brain tissue damage.

Purpose of the Study:

  • To review mitochondrial impairment during I/R.
  • To propose two distinct mechanisms of mitochondrial complex I damage.
  • To discuss potential neuroprotective strategies against I/R brain injury.

Main Methods:

  • Review of existing scientific literature on I/R and mitochondrial function.
  • Analysis of recent studies investigating mitochondrial complex I inhibition.
  • Proposal of two novel mechanisms for complex I damage.

Main Results:

  • Mitochondrial complex I is highly sensitive to I/R.
  • Mechanism 1: Reversible dissociation of flavin mononucleotide cofactor from complex I.
  • Mechanism 2: Modification of critical cysteine residues in complex I.

Conclusions:

  • These two mechanisms contribute to mitochondrial dysfunction and energy failure during I/R.
  • Understanding these processes is crucial for developing effective neuroprotective therapies.
  • Targeting complex I damage could ameliorate I/R-induced brain injury.

More Related Videos

A Flow Cytometry-based Assay for Measuring Mitochondrial Membrane Potential in Cardiac Myocytes After Hypoxia/Reoxygenation07:14

A Flow Cytometry-based Assay for Measuring Mitochondrial Membrane Potential in Cardiac Myocytes After Hypoxia/Reoxygenation

Published on: July 13, 2018

15.0K
Author Spotlight: Unveiling Oxidative Phosphorylation System Dynamics and Mitochondrial Roles in Health and Disease05:45

Author Spotlight: Unveiling Oxidative Phosphorylation System Dynamics and Mitochondrial Roles in Health and Disease

Published on: May 3, 2024

1.8K

Related Concept Videos

Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
18.3K
The Electron Transport Chain01:30

The Electron Transport Chain

The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
19.4K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
8.9K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
2.9K
Mitochondrial Membranes01:45

Mitochondrial Membranes

A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
16.5K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
11.8K