Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 17, Pages 14215-14225Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.348813
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Funding
- UK Biotechnology and Biological Sciences Research Council
- Engineering and Physical Science Research Council [BB/G009228]
- BBSRC [BB/G007519/1, BB/G009228/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G007519/1, BB/G009228/1] Funding Source: researchfish
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Little is known about enzymatic quinone-quinol interconversions in the lipid membrane when compared with our knowledge of substrate transformations by globular enzymes. Here, the smallest example of a quinol dehydrogenase in nature, CymA, has been studied. CymA is a monotopic membrane tetraheme c-type cytochrome belonging to the NapC/NirT family and central to anaerobic respiration in Shewanella sp. Using protein-film electrochemistry, it is shown that vesicle-bound menaquinone-7 is not only a substrate for this enzyme but is also required as a cofactor when converting other quinones. Here, we propose that the high concentration of quinones in the membrane negates the evolutionary pressure to create a high affinity active site. However, the instability and reactivity of reaction intermediate, semiquinone, might require a cofactor that functions to minimize damaging side reactions.
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