Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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,...
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...
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...
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,...
Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Translation accuracy in E. coli.

Nucleic acids research·2026
Same author

The Origin of Life in the Light of Evolution.

ArXiv·2026
Same author

Rapid evolution of lncRNAs introduces novel regulatory inputs into ancestral cancer pathways.

Science advances·2026
Same author

Virological investigation and comparative genomic analysis of elephant endotheliotropic herpesvirus 1B infection in an Australian captive herd of Asian elephants (Elephas maximus).

PloS one·2026
Same author

Revisiting Mitochondrial Temperature: Steady-State Heat Transfer or Non-Steady-State Dynamics?

Acta physiologica (Oxford, England)·2026
Same author

Cross-domain transfer of trehalose biosynthesis genes contributes to adaptation in high-altitude environments.

National science review·2026

Related Experiment Video

Updated: Jul 10, 2026

The Use of the Patch-Clamp Technique to Study the Thermogenic Capacity of Mitochondria
11:05

The Use of the Patch-Clamp Technique to Study the Thermogenic Capacity of Mitochondria

Published on: May 3, 2021

Decoding the Hot-Mitochondrion Paradox.

Peyman Fahimi1, Michael Lynch2, Chérif F Matta3,4,5

  • 1Department of Mathematics & Statistics, Dalhousie University, Halifax, Nova Scotia, Canada.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|July 9, 2026
PubMed
Summary
This summary is machine-generated.

Mitochondria are significantly warmer than their surroundings, defying heat conduction laws. Researchers propose ion-moving proteins act as heat engines, explaining this thermal paradox.

More Related Videos

Isolation of Mitochondria from Mouse Skeletal Muscle for Respirometric Assays
08:11

Isolation of Mitochondria from Mouse Skeletal Muscle for Respirometric Assays

Published on: February 10, 2022

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

Related Experiment Videos

Last Updated: Jul 10, 2026

The Use of the Patch-Clamp Technique to Study the Thermogenic Capacity of Mitochondria
11:05

The Use of the Patch-Clamp Technique to Study the Thermogenic Capacity of Mitochondria

Published on: May 3, 2021

Isolation of Mitochondria from Mouse Skeletal Muscle for Respirometric Assays
08:11

Isolation of Mitochondria from Mouse Skeletal Muscle for Respirometric Assays

Published on: February 10, 2022

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

Area of Science:

  • Cellular biology
  • Biophysics
  • Thermodynamics

Background:

  • Mitochondria exhibit temperatures 10°C-15°C higher than cytoplasm.
  • This observation contradicts predictions from Fourier's law of heat conduction.
  • Previous theoretical work proposed a solution to this thermal paradox.

Purpose of the Study:

  • To further explore how biological membranes, like the inner mitochondrial membrane (IMM), can maintain higher temperatures than their environment.
  • To introduce a novel heat transfer mechanism involving ion-translocating proteins.

Main Methods:

  • Modeling ion-translocating proteins in the IMM as ratchet engines.
  • Analyzing heat release during ion dehydration-translocation-hydration cycles.
  • Considering the cumulative effect of microscopic thermal events across the IMM surface.

Main Results:

  • Ion-translocating proteins may function as novel heat engines.
  • Localized heat release during ion transport contributes to temperature spikes.
  • The collective thermal activity explains elevated mitochondrial temperatures.

Conclusions:

  • A new model explains how biological membranes generate heat.
  • Ion transport proteins are key to understanding mitochondrial thermogenesis.
  • This mechanism resolves the discrepancy between observed and predicted mitochondrial temperatures.