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Volume 160, Issue 9

Structure of the respiratory chain: oxygen affinity of electron transport and the role of cytochrome peroxidase Free

Abstract

The genome of the ethanol-producing bacterium encodes a -type terminal oxidase, cytochrome complex and several -type cytochromes, yet lacks sequences homologous to any of the known bacterial cytochrome oxidase genes. Recently, it was suggested that a putative respiratory cytochrome peroxidase, receiving electrons from the cytochrome complex via cytochrome , might function as a peroxidase and/or an alternative oxidase. The present study was designed to test this hypothesis, by construction of a cytochrome peroxidase mutant (Zm6-), and comparison of its properties with those of a mutant defective in the cytochrome subunit of the complex (Zm6-). Disruption of the cytochrome peroxidase gene (ZZ60192) caused a decrease of the membrane NADH peroxidase activity, impaired the resistance of growing culture to exogenous hydrogen peroxide and hampered aerobic growth. However, this mutation did not affect the activity or oxygen affinity of the respiratory chain, or the kinetics of cytochrome reduction. Furthermore, the peroxide resistance and membrane NADH peroxidase activity of strain Zm6- had not decreased, but both the oxygen affinity of electron transport and the kinetics of cytochrome reduction were affected. It is therefore concluded that the cytochrome peroxidase does not terminate the cytochrome branch of , and that it is functioning as a quinol peroxidase.

  • Received:
  • Accepted:
  • Published Online:
Funding
This study was supported by the:
  • Latvian Council of Science (Award 536/2012 and 09.1306 )
  • Royal Society (Award TG102318)
  • Biotechnology and Biological Sciences Research Council
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2014-09-01
2024-10-05
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/content/journal/micro/10.1099/mic.0.081612-0
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Structure of the Zymomonas mobilis respiratory chain: oxygen affinity of electron transport and the role of cytochrome c peroxidase
Microbiology 160, 2045 (2014); https://doi.org/10.1099/mic.0.081612-0
/content/journal/micro/10.1099/mic.0.081612-0
/content/journal/micro/10.1099/mic.0.081612-0
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