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Applied and Environmental Microbiology, February 2007, p. 861-868, Vol. 73, No. 3
0099-2240/07/$08.00+0 doi:10.1128/AEM.01818-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Institut für Biotechnologie 1, Forschungszentrum Jülich, D-52425 Jülich, Germany
Received 2 August 2006/ Accepted 19 November 2006
Corynebacterium glutamicum possesses two terminal oxidases, cytochrome aa3 and cytochrome bd. Cytochrome aa3 forms a supercomplex with the cytochrome bc1 complex, which contains an unusual diheme cytochrome c1. Both the bc1-aa3 supercomplex and cytochrome bd transfer reducing equivalents from menaquinol to oxygen; however, they differ in their proton translocation efficiency by a factor of three. Here, we analyzed the role of cytochrome bd for growth and lysine production. When cultivated in glucose minimal medium, a cydAB deletion mutant of C. glutamicum ATCC 13032 grew like the wild type in the exponential phase, but growth thereafter was inhibited, leading to a biomass formation 40% less than that of the wild type. Constitutive overproduction of functional cytochrome bd oxidase in ATCC 13032 led to a reduction of the growth rate by
45% and of the maximal biomass by
35%, presumably as a consequence of increased electron flow through the inefficient cytochrome bd oxidase. In the L-lysine-producing C. glutamicum strain MH20-22B, deletion of the cydAB genes had only minor effects on growth rate and biomass formation, but lysine production was increased by
12%. Thus, the respiratory chain was shown to be a target for improving amino acid production by C. glutamicum.
Published ahead of print on 1 December 2006.
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