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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Fast Reactions01:27

Fast Reactions

Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...

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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Ultrafast proteinquake dynamics in cytochrome c.

Chen Zang1, Jeffrey A Stevens, Justin J Link

  • 1Department of Physics, Program of Biophysics, The Ohio State University, 191 West Woodruff Avenue, Columbus, Ohio, 43210, USA.

Journal of the American Chemical Society
|February 11, 2009
PubMed
Summary
This summary is machine-generated.

Cytochrome c

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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Area of Science:

  • Biochemistry
  • Protein Dynamics
  • Spectroscopy

Background:

  • Cytochrome c is a crucial protein in cellular respiration.
  • Understanding its redox states and dynamics is key to cellular function.

Purpose of the Study:

  • To investigate the distinct heme dynamics and protein conformational changes in ferric and ferrous cytochrome c.
  • To elucidate the ultrafast processes following femtosecond excitation.

Main Methods:

  • Femtosecond spectroscopy with visible to UV probing wavelengths.
  • Site-directed mutagenesis of cytochrome c.
  • Analysis of heme coordination and protein relaxation dynamics.

Main Results:

  • Ferrous cytochrome c exhibits ultrafast heme ligand dissociation (6-fold to 5-fold coordination) and subsequent rebinding (7 ps), inducing proteinquakes and global conformational changes (recovery in 13 and 42 ps).
  • Ferric cytochrome c maintains 6-fold heme coordination, with dynamics limited to local site processes (internal conversion, vibrational cooling) and complete ground-state recovery in 10 ps, showing no global relaxation.
  • Protein dynamics differ significantly between the two redox states.

Conclusions:

  • The redox state of cytochrome c dictates its ultrafast dynamics and conformational relaxation pathways.
  • Ferrous state dynamics involve significant heme coordination changes and large-scale protein perturbations, unlike the ferric state.
  • These findings provide critical insights into the functional mechanisms of cytochrome c.