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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

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Published on: October 15, 2019

The Rieske/cytochrome b complex of Heliobacteria.

A L Ducluzeau¹, E Chenu, L Capowiez

¹Laboratoire de Bioénergétique et Ingénierie des protéines, Institut de Biologie Structurale et Microbiologie, Unité Propre de Recherche 9036, Centre National de la Recherche Scientifique, 31, chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.

Biochimica Et Biophysica Acta

|May 14, 2008

Summary

This summary is machine-generated.

Heliobacteria possess a unique Rieske/cytochrome b complex featuring a covalently attached heme c(i). This heme exhibits distinct EPR signatures in Heliobacterium modesticaldum and Heliobacillus mobilis, suggesting a protonatable amino acid ligand.

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Area of Science:

Molecular Biology
Biochemistry
Bioenergetics

Background:

Heliobacteria contain a Rieske/cytochrome b complex, structurally similar to the b(6)f complex found in cyanobacteria and chloroplasts.
A key difference lies in the di-heme cytochrome c component of the Heliobacteria complex.

Purpose of the Study:

To investigate the nature and properties of the heme c(i) within the Heliobacteria Rieske/cytochrome b complex.
To compare the heme c(i) characteristics with those in the related b(6)f complex.

Main Methods:

Biochemical analyses were performed on the Heliobacteria Rieske/cytochrome b complex.
Biophysical studies, including Electron Paramagnetic Resonance (EPR) spectroscopy, were utilized.
The study examined two species: Heliobacterium modesticaldum and Heliobacillus mobilis.

Main Results:

Biochemical and biophysical evidence confirmed the covalent attachment of a heme c(i) to the Rieske/cytochrome b complex in Heliobacteria.
EPR spectroscopy revealed a strong axial ligand for the heme c(i) in both studied species.
This ligand is distinct from the b(6)f complex and is likely a protonatable amino acid residue.

Conclusions:

The Heliobacteria Rieske/cytochrome b complex possesses a unique heme c(i) with a specific axial ligand.
This finding highlights structural and functional divergence from the canonical b(6)f complex.
Further research into this unique heme environment could elucidate novel electron transfer mechanisms.