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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...
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...
Redox Reactions01:27

Redox Reactions

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Coordination Number and Geometry

For transition metal complexes, the coordination number determines the geometry around the central metal ion. Table 1 compares coordination numbers to molecular geometry. The most common structures of the complexes in coordination compounds are octahedral, tetrahedral, and square planar.
Structural Isomerism02:34

Structural Isomerism

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Related Experiment Video

Updated: Jul 16, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Published on: December 4, 2017

Structure and function of a hexameric copper-containing nitrite reductase.

Masaki Nojiri1, Yong Xie, Tsuyoshi Inoue

  • 1Department of Chemistry, Graduate School of Science, Osaka University, Osaka 560-0043, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|March 16, 2007
PubMed
Summary

The crystal structure of copper-containing nitrite reductase (NIR) from Hyphomicrobium denitrificans was determined. This key denitrification enzyme

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Last Updated: Jul 16, 2026

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Published on: September 7, 2019

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Dissimilatory nitrite reductase (NIR) is crucial for denitrification, converting nitrite to gaseous nitrogen products.
  • Understanding NIR structure and function is vital for microbial ecology and biogeochemical cycles.

Purpose of the Study:

  • Determine the crystal structure of copper-containing nitrite reductase from Hyphomicrobium denitrificans.
  • Elucidate the structural basis for NIR's catalytic activity and electron transfer mechanisms.

Main Methods:

  • X-ray crystallography at 2.2-A resolution.
  • Biochemical analysis of enzyme structure and function.

Main Results:

  • The Hyphomicrobium denitrificans NIR forms a hexameric structure composed of three copper atoms.
  • Detailed structural analysis revealed the organization of cupredoxin domains and copper-binding sites.
  • Type 1 copper facilitates electron transfer, while type 2 copper is involved in substrate binding and reduction.

Conclusions:

  • The determined crystal structure provides insights into the catalytic mechanism of nitrite reduction.
  • Structural features explain the intermolecular electron transfer from cytochrome c(550) to NIR.
  • This study advances our understanding of denitrification pathways in methylotrophic bacteria.