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Related Concept Videos

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...
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Color in Coordination Complexes
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Related Experiment Video

Updated: Jul 14, 2026

[(DPEPhos)(bcp)Cu]PF6: A General and Broadly Applicable Copper-Based Photoredox Catalyst
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A new dinuclear heme-copper complex derived from functionalized protoporphyrin IX.

Corrado Dallacosta1, Wendel A Alves, Ana M da Costa Ferreira

  • 1Dipartimento di Chimica Generale, Università di Pavia, Via Taramelli 12, 27100 Pavia, Italy.

Dalton Transactions (Cambridge, England : 2003)
|May 22, 2007
PubMed
Summary

This study introduces a novel biomimetic model of respiratory oxidases, featuring a heme/copper center. The model demonstrates cooperative interactions between iron and copper in binding azide and reacting with hydrogen peroxide and dioxygen.

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Area of Science:

  • Biomimetic Chemistry
  • Bioinorganic Chemistry
  • Enzyme Mechanisms

Background:

  • Respiratory oxidases contain a crucial heterodinuclear heme/copper active site.
  • Understanding the cooperative function of these metal centers is vital for deciphering biological electron transfer and oxygen reduction.

Purpose of the Study:

  • To develop a novel biomimetic model of the heterodinuclear heme/copper center in respiratory oxidases.
  • To investigate the cooperative reactivity of the iron and copper centers with small molecules like azide, hydrogen peroxide, and dioxygen.

Main Methods:

  • Synthesis of iron(III) protoporphyrin IX derivatives with appended Gly-L-His-OMe and amino-bis(benzimidazole) ligands.
  • Complexation with copper(II) or copper(I) ions to form Fe(III)/Cu(II) and Fe(II)/Cu(I) biomimetic models.
  • Spectroscopic studies (UV-Vis) of azide binding, hydrogen peroxide adducts, and dioxygen reactivity at low temperatures.
  • Enzymatic activity assays (peroxidase) using p-cresol phenol coupling to evaluate catalytic performance at different pH values.

Main Results:

  • A biomimetic model, Fe(III)/Cu(II) complex 2, was synthesized, exhibiting stronger azide binding than the iron-only complex 1.
  • Cooperative effects were observed in hydrogen peroxide reactions, with distinct optical features for peroxide adducts of complexes 1 and 2.
  • The Cu(II) ion enhanced peroxidase activity at acidic pH by facilitating O-O bond cleavage but decreased it at basic pH.
  • Reduced complexes showed slightly different spectral properties upon reaction with dioxygen, indicating copper's involvement.

Conclusions:

  • The synthesized biomimetic model effectively mimics aspects of the heterodinuclear heme/copper center's function.
  • Cooperative interactions between iron and copper centers significantly influence the reactivity towards azide, hydrogen peroxide, and dioxygen.
  • The model provides insights into the pH-dependent catalytic mechanisms of respiratory oxidases.