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Related Experiment Video

Updated: May 13, 2026

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Published on: June 1, 2017

Conformation-specific crosslinking of mitochondrial complex I.

Margherita Ciano¹, Matthew Fuszard, Heinrich Heide

¹Queen's University Belfast, School of Biological Sciences, Medical Biology Centre, Belfast, UK.

|March 5, 2013

Summary

Researchers used a crosslinker to study mitochondrial complex I, finding that the ND3 and NDUFA9 subunits interact in the de-active form but not the active form. This reveals insights into the enzyme's conformational changes and energy transduction.

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Last Updated: May 13, 2026

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Hybrid Clear/Blue Native Electrophoresis for the Separation and Analysis of Mitochondrial Respiratory Chain Supercomplexes

Published on: May 19, 2019

Area of Science:

Biochemistry
Structural Biology
Mitochondrial Function

Background:

Mitochondrial complex I is crucial for the eukaryotic respiratory chain.
Complex I exhibits an active/de-active conformational transition.
High-resolution structures of complex I are currently unavailable.

Purpose of the Study:

To investigate the structural differences between the active (A) and de-active (D) forms of mitochondrial complex I.
To identify interacting subunits in the de-active form of complex I using chemical crosslinking.

Main Methods:

Utilized an amine- and sulfhydryl-reactive crosslinker (SPDP) of 6.8Å length.
Analyzed crosslinking patterns between subunits in both active and de-active forms of complex I.

Main Results:

The ND3 subunit was found to crosslink with the NDUFA9 subunit specifically in the de-active (D) form of complex I.
This crosslinking was not observed in the active (A) form, indicating a conformational change.
The interacting subunits are likely located in a critical junction region involved in ubiquinone binding and energy transduction.

Conclusions:

The ND3 and NDUFA9 subunits are in close proximity in the de-active conformation of mitochondrial complex I.
This interaction highlights a structural rearrangement associated with the enzyme's conformational transition.
The findings provide insights into the mechanism of energy transduction and substrate ubiquinone binding in complex I.