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

Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

9.6K
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...
9.6K
The Electron Transport Chain01:30

The Electron Transport Chain

21.0K
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...
21.0K
Decreased Body Temperature01:29

Decreased Body Temperature

1.1K
A decreased body temperature can occur in patients with hypothermia and frostbite. Heat loss with extended cold exposure overpowers the body's ability to create heat, resulting in hypothermia. Core temperature readings help classify hypothermia. Mild hypothermia is temperatures between 32 °C (89.6 °F) and 35°C (95 °F) and is caused by impaired thermoregulation. Moderate hypothermia is temperatures between 28 C (82.4 °F) and 32 °C (89.6 °F) caused by...
1.1K
Effect of Temperature Change on Reaction Rate02:28

Effect of Temperature Change on Reaction Rate

5.3K
The Arrhenius equation,
5.3K
Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.5K
Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
4.5K
Responses to Heat and Cold Stress02:45

Responses to Heat and Cold Stress

15.6K
Every organism has an optimum temperature range within which healthy growth and physiological functioning can occur. At the ends of this range, there will be a minimum and maximum temperature that interrupt biological processes.
15.6K

You might also read

Related Articles

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

Sort by
Same author

Pattern formation in a tunable medium: the Belousov-Zhabotinsky reaction in an aerosol OT microemulsion.

Physical review letters·2001
Same author

Poly(oxazolines)s with tapered minidendritic side groups. The simplest cylindrical models to investigate the formation of two-dimensional and three-dimensional order by direct visualization.

Biomacromolecules·2001
Same author

Inwardly rotating spiral waves in a reaction-diffusion system.

Science (New York, N.Y.)·2001
Same author

[Quantum transitions between states and cosmophysical fluctuations].

Biofizika·2001
Same author

Synthesis and spectroscopic studies of non-heme diiron(III) species with a terminal hydroperoxide ligand: models for hemerythrin.

Inorganic chemistry·2001
Same author

Oscillatory clusters in the periodically illuminated, spatially extended Belousov-Zhabotinsky reaction.

Physical review letters·2001

Related Experiment Video

Updated: Mar 18, 2026

Author Spotlight: Preservation of Bioenergetic Parameters in Peripheral Blood Mononuclear Cells After Cryopreservation
04:10

Author Spotlight: Preservation of Bioenergetic Parameters in Peripheral Blood Mononuclear Cells After Cryopreservation

Published on: October 20, 2023

2.4K

[Low temperature reduction of cytochrome c complexes].

S N Magonov, L A Bliumenfel'd, V K Vanag

    Biofizika
    |May 1, 1978
    PubMed
    Summary
    This summary is machine-generated.

    Investigating ferricytochrome c complexes with azide, imidazole, and cyanide at liquid nitrogen temperatures revealed distinct absorption spectra upon reduction. These spectral differences suggest axial ligation of iron by exogenous ligands, which are removed upon warming.

    More Related Videos

    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

    2.3K
    In vitro Assessment of Myocardial Protection following Hypothermia-Preconditioning in a Human Cardiac Myocytes Model
    08:22

    In vitro Assessment of Myocardial Protection following Hypothermia-Preconditioning in a Human Cardiac Myocytes Model

    Published on: October 27, 2020

    3.5K

    Related Experiment Videos

    Last Updated: Mar 18, 2026

    Author Spotlight: Preservation of Bioenergetic Parameters in Peripheral Blood Mononuclear Cells After Cryopreservation
    04:10

    Author Spotlight: Preservation of Bioenergetic Parameters in Peripheral Blood Mononuclear Cells After Cryopreservation

    Published on: October 20, 2023

    2.4K
    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

    2.3K
    In vitro Assessment of Myocardial Protection following Hypothermia-Preconditioning in a Human Cardiac Myocytes Model
    08:22

    In vitro Assessment of Myocardial Protection following Hypothermia-Preconditioning in a Human Cardiac Myocytes Model

    Published on: October 27, 2020

    3.5K

    Area of Science:

    • Biochemistry
    • Spectroscopy
    • Electron transfer reactions

    Background:

    • Cytochrome c is a crucial protein in electron transport.
    • Understanding ligand interactions with cytochrome c is vital for elucidating its function.
    • Low-temperature spectroscopy provides insights into transient species and reaction mechanisms.

    Purpose of the Study:

    • To investigate the absorption spectra of ferricytochrome c complexes with azide, imidazole, and cyanide.
    • To study the effect of trapped electrons and radiation-induced reduction on these complexes.
    • To understand the role of exogenous ligands in the electronic structure of ferrocytochrome c.

    Main Methods:

    • Absorption spectroscopy at liquid nitrogen temperature (77 K).
    • Reduction of ferricytochrome c complexes using trapped electrons generated by radiation.
    • Comparative spectral analysis of reduced complexes and ferrocytochrome c.

    Main Results:

    • Distinct absorption spectra were observed for reduced ferricytochrome c complexes compared to ferrocytochrome c.
    • Spectral differences were attributed to the axial ligation of Fe(II) by exogenous ligands (azide, imidazole, cyanide).
    • Ligand dissociation from Fe(II) was observed upon increasing the temperature from 77 K.

    Conclusions:

    • Axial ligation of ferrocytochrome c by exogenous ligands significantly alters its absorption spectrum.
    • The binding of azide, imidazole, and cyanide to ferrocytochrome c is temperature-dependent.
    • Low-temperature spectroscopy is a powerful tool for characterizing ligand interactions in metalloproteins.