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Related Concept Videos

Redox Reactions01:27

Redox Reactions

Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
Redox Reactions01:24

Redox Reactions

Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
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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 Equilibria: Overview01:23

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A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...
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Related Experiment Video

Updated: Jun 24, 2026

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

Redox-dependent dynamics in cytochrome P450cam.

Susan Sondej Pochapsky1, Marina Dang, Bo OuYang

  • 1Department of Chemistry, Brandeis University, 415 South Street, MS 015, Waltham, Massachusetts 02454-9110, USA.

Biochemistry
|April 16, 2009
PubMed
Summary
This summary is machine-generated.

The oxidation state of the heme iron in cytochrome P450(cam) (CYP101) influences protein dynamics. Reduced CYP101 shows less motion, particularly in substrate access and effector binding regions, impacting enzyme function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Cytochrome P450(cam) (CYP101) is a camphor hydroxylase crucial for drug metabolism and biodegradation.
  • Protein backbone dynamics are known to be influenced by the heme iron's oxidation and ligation state.

Purpose of the Study:

  • To investigate how the oxidation state of the heme iron affects the local protein backbone dynamics of CYP101.
  • To compare dynamics between oxidized and reduced forms of CYP101 using nuclear magnetic resonance (NMR) spectroscopy.

Main Methods:

  • Utilized (1)H-(15)N correlation NMR experiments.
  • Employed hydrogen-deuterium (H-D) exchange kinetics and (15)N relaxation measurements.
  • Compared NMR data with prior H-D exchange mass spectrometry results.

Main Results:

  • The reduced form of CYP101 exhibits lower-amplitude motions in secondary structural elements compared to the oxidized form.
  • These dynamic differences are more significant in regions critical for substrate access (B' helix, beta3/beta5 sheets) and putidaredoxin binding (C/L helices).

Conclusions:

  • Changes in heme iron oxidation state locally affect protein structure and dynamics in CYP101.
  • Observed dynamic alterations are relevant to the enzyme's catalytic mechanism and substrate binding interactions.