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Updated: Jun 16, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
Heliobacterial Rieske/cytb complex
1BIP, Centre National de la Recherche Scientifique, UPR9036, IFR88, 31 Chemin Joseph Aiguier, Marseille, France. baymann@ifr88.cnrs-mrs.fr.
Insights
The Heliobacteria Rieske/cytochrome b complex shares similarities with the b6f complex, featuring unique cofactor content and redox potentials. Its role in cyclic electron transfer is crucial for photosynthesis.
Area of Science:
- Biochemistry
- Photosynthesis research
- Microbial metabolism
Background:
- Rieske/cytochrome b complex structure and function in Heliobacteria are poorly understood.
- Heliobacteria's phylogenetic position suggests a relationship to the b6f complex.
- The complex includes a diheme cytochrome c, Rieske iron-sulfur protein, and transmembrane cytochrome b.
Purpose of the Study:
- To elucidate the structure and function of the Heliobacteria Rieske/cytochrome b complex.
- To compare its properties with the well-characterized b6f complex.
- To understand its role in photosynthetic electron transfer.
Main Methods:
- Phylogenetic analysis to infer structural relationships.
- Spectroscopic methods to determine cofactor content and redox potentials.
- Biochemical assays to investigate enzyme activity.
Main Results:
- The Heliobacteria complex contains heme c(i) in the Q(i) binding pocket, similar to b6f complexes.
- Redox midpoint potentials are more negative than in b6f complexes, aligning with its reaction partners.
- The enzyme participates in cyclic electron transfer around Photosystem I (RCI).
Conclusions:
- The Heliobacteria Rieske/cytochrome b complex is structurally and functionally related to the b6f complex.
- Its unique cofactor and redox properties are adapted to its specific photosynthetic environment.
- Despite challenges like oxygen sensitivity, functional studies are feasible and informative.
Abstract:
Data on structure and function of the Rieske/cytb complex from Heliobacteria are scarce. They indicate that the complex is related to the b (6) f complex in agreement with the phylogenetic position of the organism. It is composed of a diheme cytochrome c, and a Rieske iron-sulfur protein, together with transmembrane cytochrome b (6) and subunit IV. Additional small subunits may be part of the complex. The cofactor content comprises heme c (i), first discovered in the Q(i) binding pocket of b (6) f complexes. The redox midpoint potentials are more negative than in b (6) f complex in agreement with the lower redox midpoint potentials (by about 150 mV) of its reaction partners, menaquinone, and cytochrome c (553). The enzyme is implicated in cyclic electron transfer around the RCI. Functional studies are favored by the absence of antennae and the simple photosynthetic reaction chain but are hampered by the high oxygen sensitivity of the organism, its chlorophyll, and lipids.
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