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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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Updated: Jun 6, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

Faster interprotein electron transfer in a [myoglobin, b⁵] complex with a redesigned interface.

Peng Xiong1, Judith M Nocek, Josh Vura-Weis

  • 1Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208-3113, USA.

Science (New York, N.Y.)
|November 25, 2010
PubMed
Summary

Electron transfer rates between myoglobin and cytochrome b(5) were measured and found to be very fast. Simulations revealed protein binding configurations that explain these rapid electron transfer dynamics.

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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

Area of Science:

  • Biochemistry
  • Protein-protein interactions
  • Electron transfer dynamics

Background:

  • Physiological protein partners myoglobin (Mb) and cytochrome b(5) (b(5)) are crucial for biological electron transfer.
  • Understanding interprotein electron transfer (ET) is key to fields like photosynthesis and cellular respiration.
  • Redesigning protein interfaces can modulate ET kinetics.

Purpose of the Study:

  • To directly measure electron transfer rates in a redesigned myoglobin-cytochrome b(5) complex.
  • To investigate the structural basis of interprotein electron transfer using Brownian dynamics simulations.
  • To compare measured ET rates with those in natural systems like the photosynthetic reaction center.

Main Methods:

  • Engineered a protein-protein complex by mutating surface residues of myoglobin.
  • Employed direct measurements to quantify interprotein electron transfer rates.
  • Utilized Brownian dynamics simulations to model protein binding configurations and ET pathways.

Main Results:

  • Achieved interprotein ET rates comparable to those in the photosynthetic reaction center.
  • Identified an ensemble of binding configurations for the myoglobin-cytochrome b(5) complex.
  • Observed distributed kinetics for charge-separation and charge-recombination ET.
  • Median rate constants for forward (k(f)(s)) and backward (k(b)(s)) ET were 2.1 × 10^9 s⁻¹ and 4.3 × 10^10 s⁻¹, respectively.

Conclusions:

  • Engineered protein interfaces can facilitate highly efficient interprotein electron transfer.
  • The observed ET rates approach those of the initial charge separation in photosynthesis.
  • Structural flexibility and distributed configurations play a significant role in ET kinetics.