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Related Concept Videos

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...
Electron Transport Chain Components01:29

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The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
Electron Transport Chains01:28

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The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...
The Supercomplexes in the Crista Membrane01:41

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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...
Electron Transport Chain: Complex I and II01:46

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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.
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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Dynamics in electron transfer protein complexes.

Qamar Bashir1, Sandra Scanu, Marcellus Ubbink

  • 1Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, The Netherlands.

The FEBS Journal
|March 1, 2011
PubMed
Summary
This summary is machine-generated.

Electron transfer proteins form transient complexes, balancing initial low-specificity binding with specific interactions for efficient electron transfer and rapid turnover.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Electron transfer proteins are crucial for shuttling electrons between redox enzymes.
  • The protein complexes involved are highly transient, necessitating rapid formation and dissociation.
  • Understanding these interactions is key to elucidating cellular energy transfer mechanisms.

Purpose of the Study:

  • To investigate the role and characteristics of the encounter state in electron transfer protein complexes.
  • To explore how the balance between encounter complexes and specific complexes impacts biological function.
  • To provide insights into the dynamics of transient protein-protein interactions.

Main Methods:

  • Paramagnetic relaxation enhancement (PRE) NMR spectroscopy.
  • Chemical shift perturbation (CSP) analysis.
  • Characterization of transient protein-protein interactions and encounter states.

Main Results:

  • The encounter state, dominated by electrostatics, plays a significant role in initial protein binding.
  • The surface area involved in the encounter state can be limited, sometimes showing no specific binding.
  • Encounter complexes can constitute a substantial fraction of the interaction, especially in smaller complexes.

Conclusions:

  • A delicate balance exists between the low-specificity encounter state and the high-specificity productive complex.
  • This balance is essential for meeting the opposing demands of rapid electron transfer and high complex turnover rates.
  • The encounter state dynamics are critical for the functional efficiency of electron transfer protein complexes.