Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Cecchini, G. et al.

Oxidation of reduced menaquinone by the fumarate reductase complex in Escherichia coli requires the hydrophobic FrdD peptide.

Plasmids carrying cloned segments of the frd operon of Escherichia coli have been used in genetic complementation studies to identify two independent mutants defective in the frdD gene, which encodes the hydrophobic FrdD polypeptide of the fumarate reductase complex. Mutations in the frdA and frdB genes have also been mapped by this technique. One of the FrdD peptide mutants, DW109 (frdD-109), showed that fumarate reductase was not as tightly bound to the membrane in this mutant. In addition, the mutation in the FrdD peptide caused an almost total loss of the ability of the enzyme to oxidize either menaquinol-6, a physiological donor for fumarate reduction, or reduced benzyl viologen. However, the mutation did not impair the ability of the membrane-bound fumarate reductase complex to function with succinate as substrate, as evidenced by unchanged turnover numbers for phenazine methosulfate and 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone (a quinone analogue) reductase activities. These data establish the essential role of the FrdD polypeptide both in the interaction of the enzyme with reduced menaquinone and thus in anaerobic respiration with fumarate as electron acceptor, and in binding the enzyme to the membrane.[1]

References

Oxidation of reduced menaquinone by the fumarate reductase complex in Escherichia coli requires the hydrophobic FrdD peptide. Cecchini, G., Thompson, C.R., Ackrell, B.A., Westenberg, D.J., Dean, N., Gunsalus, R.P. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]

Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.