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Electron Transport Chain: Complex III and IV

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...

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Electron Transport Chain: Complex I and II

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Related Experiment Video

Updated: May 15, 2026

Measuring Trans-Plasma Membrane Electron Transport by C2C12 Myotubes

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Published on: May 4, 2018

Cytochromes b561: ascorbate-mediated trans-membrane electron transport.

Han Asard¹, Raffaella Barbaro, Paolo Trost

¹Department of Biology, University of Antwerp, Antwerp, Belgium. han.asard@ua.ac.be

Antioxidants & Redox Signaling

|December 20, 2012

Summary

Cytochromes b561 (CYB561s) are essential di-heme proteins involved in vital cellular processes. Their diverse roles in plants and animals, including iron metabolism and neurological functions, highlight their broad physiological significance.

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Last Updated: May 15, 2026

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Published on: April 11, 2014

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Area of Science:

Biochemistry
Molecular Biology

Background:

Cytochromes b561 (CYB561s) are trans-membrane, di-heme proteins found in diverse organisms.
Their ubiquitous nature and unique "two-heme four-helix" structure are recently recognized.
Dopamine β-monooxygenase (DOMON) domains in CYBDOM proteins may contain an additional heme b.

Purpose of the Study:

To provide an overview of the various roles and structural properties of newly identified CYB561 proteins.
To elucidate the physiological functions of CYB561s and CYBDOMs in plants and animals.

Main Methods:

Study of recombinant CYB561 proteins to reveal structural and functional properties.
Identification of new CYB561 proteins.

Main Results:

CYB561s function as monodehydroascorbate reductases and Fe³⁺-reductases.
CYB561s and CYBDOMs support stress defense, cell wall modification, iron metabolism, tumor suppression, and neurological processes.
CYB561s broaden the understanding of ascorbate (ASC) physiological roles.

Conclusions:

Mutant studies will further detail CYB561 and CYBDOM mechanisms in cellular metabolism.
Heterologous expression systems will enable protein crystallization and atomic-level structural insights.
Further research will illuminate the intra-molecular electron transport mechanisms of CYB561s.