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Videos de Conceptos Relacionados

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...
Electron Transport Chain Components01:29

Electron Transport Chain Components

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 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: 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...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...

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Video Experimental Relacionado

Updated: Jul 12, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

Las vías de túnel de electrones en el citocromo C.

D S Wuttke, M J Bjerrum, J R Winkler

    Science (New York, N.Y.)
    |May 15, 1992
    PubMed
    Resumen

    Se midieron los acoplamientos electrónicos entre el hierro y el rutenio en los derivados del citocromo c. Estos acoplamientos se correlacionan con las longitudes de las vías de transferencia de electrones, no solo con la distancia, con saltos a través del espacio que reducen significativamente la fuerza del acoplamiento.

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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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    Last Updated: Jul 12, 2026

    Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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    Published on: September 14, 2014

    Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
    08:37

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

    Published on: June 1, 2017

    Área de la Ciencia:

    • La bioquímica es la bioquímica.
    • Química Física es la química física.
    • La biofísica molecular es la biofísica molecular.

    Sus antecedentes:

    • El citocromo c es una proteína crucial en el transporte de electrones.
    • Comprender los mecanismos de transferencia de electrones es vital para los procesos biológicos.
    • Los residuos de histidina juegan un papel clave en la coordinación de los iones metálicos y en la mediación de la transferencia de electrones.

    Objetivo del estudio:

    • Para cuantificar acoplamientos electrónicos distantes entre Fe2+) y Ru3+) en el citocromo c modificado.
    • Para investigar la relación entre los acoplamientos electrónicos, la longitud de la vía y la distancia.
    • Para dilucidar el impacto de los saltos a través del espacio en las vías de transferencia de electrones.

    Principales métodos:

    • Mediciones de la velocidad de transferencia de electrones intramoleculares en los derivados del citocromo c Ru (histidina) (x).
    • Análisis de acoplamientos electrónicos basados en tasas experimentales.
    • Correlación de los acoplamientos con las distancias histidina-hema y las longitudes de las vías de túnel sigma.

    Principales resultados:

    • Los acoplamientos electrónicos se extrajeron y cuantificaron con éxito para cuatro derivados del citocromo c.
    • El orden de los acoplamientos no se alineó con las distancias simples borde-borde histidina-hema.
    • Acoplamientos correlacionados con la longitud de las vías de túnel sigma, incluyendo enlaces covalentes, enlaces de hidrógeno y saltos a través del espacio.
    • Un salto específico a través del espacio (Pro71 a Met80) aumentó significativamente la longitud de la trayectoria y disminuyó el acoplamiento para His72.

    Conclusiones:

    • Los acoplamientos de transferencia de electrones son sensibles a la estructura detallada de la vía de túnel, no sólo a la distancia.
    • Los saltos a través del espacio representan barreras significativas que reducen la fuerza del acoplamiento electrónico.
    • Este estudio proporciona información sobre los factores que rigen la transferencia de electrones de largo alcance en las metaloproteínas.