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Interactive Molecular Model Assembly with 3D Printing

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The alternative complex III: a different architecture using known building modules.

Patrícia N Refojo¹, Filipa L Sousa, Miguel Teixeira

¹Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN, 2780-157 Oeiras, Portugal.

Biochimica Et Biophysica Acta

|April 27, 2010

Summary

This summary is machine-generated.

Alternative complex III (ACIII) is a newly discovered enzyme involved in electron transfer, distinct from the well-known cytochrome bc1 complex. Its genes are widespread in bacteria, suggesting a significant role in microbial respiration.

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Area of Science:

Biochemistry
Microbiology
Genomics

Background:

Cytochrome bc1 complexes were historically the sole known enzymes facilitating electron transfer from reduced quinones to cytochrome c.
A novel enzyme, alternative complex III (ACIII), with similar activity but unique subunit composition, was identified in Rhodothermus marinus membranes.
ACIII has since been biochemically, spectroscopically, and genetically characterized.

Purpose of the Study:

To provide a comprehensive overview of current knowledge regarding alternative complex III (ACIII).
To investigate the evolutionary relationship between ACIII and the complex iron-sulfur molybdoenzyme family.
To analyze the distribution of ACIII genes across sequenced bacterial genomes.

Main Methods:

Purification and characterization of ACIII from Rhodothermus marinus membranes.
Biochemical, spectroscopic, and genetic analyses of ACIII.
Bioinformatic analysis of completely sequenced genomes to identify ACIII-related genes and investigate evolutionary connections.

Main Results:

ACIII was purified and characterized, revealing a unique subunit composition.
The genes encoding ACIII were found to be widespread, particularly within the Bacteria domain, indicating it is not exclusive to R. marinus.
Genomic analysis suggests ACIII represents a novel combination of modules found in other respiratory complexes, with potential links to the complex iron-sulfur molybdoenzyme family.

Conclusions:

Alternative complex III (ACIII) is a significant enzyme in microbial respiration, with a broader distribution than initially thought.
ACIII represents a novel respiratory complex formed by a unique assembly of known protein modules.
Further research into ACIII's function and evolutionary history is warranted.