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Related Concept Videos

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,...
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,...
Electron Transport Chains01:28

Electron Transport Chains

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 Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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,...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...

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Related Experiment Video

Updated: Jul 7, 2026

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models
08:48

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models

Published on: June 30, 2023

Electrical properties and structural transitions in the mitochondrion.

D D Eley1, N C Lockhart, C N Richardson

  • 1Department of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD.

Journal of Bioenergetics and Biomembranes
|October 1, 1977
PubMed
Summary

Mitochondrial charge transport involves both electronic carriers and polarization. A key transition temperature was identified, correlating conductivity with phospholipid reorientation and interfacial polarization.

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Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
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Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

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Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue
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Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue

Published on: March 23, 2015

Related Experiment Videos

Last Updated: Jul 7, 2026

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models
08:48

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models

Published on: June 30, 2023

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
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Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Published on: June 1, 2017

Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue
09:27

Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue

Published on: March 23, 2015

Area of Science:

  • Biophysics
  • Materials Science
  • Mitochondrial Research

Background:

  • Mitochondrial function relies on charge transport within lipoprotein systems.
  • Understanding charge carrier mechanisms is crucial for cellular energy processes.

Purpose of the Study:

  • To investigate charge carrier generation and transport in mitochondrial lipoproteins.
  • To correlate electrical properties with morphological and structural changes.
  • To characterize the nature of charge carriers.

Main Methods:

  • Electrical conductivity measurements.
  • Low-frequency dielectric relaxation analysis.
  • Thermoelectric power (Seebeck coefficient) determination.
  • Differential Thermal Analysis (DTA) and Nuclear Magnetic Resonance (NMR) for structural analysis.

Main Results:

  • A consistent transition temperature was observed across all techniques.
  • Steady-state conductivity below the transition is linked to phospholipid main chain reorientation.
  • Above the transition, conductivity correlates with interfacial polarization.
  • The Seebeck coefficient confirmed the electronic nature of the charge carriers.
  • Cytochrome oxidase analysis revealed ionic impurities, not intrinsic charge transport behavior.

Conclusions:

  • Charge transport in mitochondrial lipoproteins is a complex process involving both free charge carriers and polarization phenomena.
  • A distinct transition temperature marks a change in the dominant charge transport mechanism.
  • Electronic charge carriers are fundamental to mitochondrial function.