@article{fdi:010064148,
  title = {{G}rowth of theobligate anaerobe {D}esulfovibrio vulgaris {H}ildenborough under continuous low oxygen concentration sparging : impact of the membrane- bound oxygen reductases},
  author = {{R}amel, {F}. and {B}rasseur, {G}. and {P}ieulle, {L}. and {V}alette, {O}. and {H}irschler-{R}{\'e}a, {A}. and {F}ardeau, {M}arie-{L}aure and {D}olla, {A}.},
  editor = {},
  language = {{ENG}},
  abstract = {{A}lthough obligate anaerobe, the sulfate-reducing bacterium {D}esulfovibrio vulgaris {H}ilden-borough ({D}v{H}) exhibits high aerotolerance that involves several enzymatic systems, including two membrane-bound oxygen reductases, a bd-quinol oxidase and a cc(b/o)o(3) cytochrome oxidase. {E}ffect of constant low oxygen concentration on growth and morphology of the wild-type, single ({D}elta bd,{D}elta cox) and double deletion ({D}elta coxbd) mutant strains of the genes encoding these oxygen reductases was studied. {W}hen both wild-type and deletion mutant strains were cultured in lactate/sulfate medium under constant 0.02% {O}-2 sparging, they were able to grow but the final biomasses and the growth yield were lower than that obtained under anaerobic conditions. {A}t the end of the growth, lactate was not completely consumed and when conditions were then switched to anaerobic, growth resumed. {T}ime-lapse microscopy revealed that a large majority of the cells were then able to divide (over 97%) but the time to recover a complete division event was longer for single deletion mutant {D}elta bd than for the three other strains. {D}etermination of the molar growth yields on lactate suggested that a part of the energy gained from lactate oxidation was derived toward cells protection/repairing against oxidative conditions rather than biosynthesis, and that this part was higher in the single deletion mutant {D}elta bd and, to a lesser extent, {D}elta cox strains. {O}ur data show that when {D}v{H} encounters oxidative conditions, it is able to stop growing and to rapidly resume growing when conditions are switched to anaerobic, suggesting that it enters active dormancy sate under oxidative conditions. {W}e propose that the pyruvate-ferredoxin oxidoreductase ({PFOR}) plays a central role in this phenomenon by reversibly switching from an oxidative-sensitive fully active state to an oxidative-insensitive inactive state. {T}he oxygen reductases, and especially the bd-quinol oxidase, would have a crucial function by maintaining reducing conditions that permit {PFOR} to stay in its active state.},
  keywords = {},
  booktitle = {},
  journal = {{P}los {O}ne},
  volume = {10},
  numero = {4},
  pages = {e0123455 [17 p.]},
  ISSN = {1932-6203},
  year = {2015},
  DOI = {10.1371/journal.pone.0123455},
  URL = {https://www.documentation.ird.fr/hor/fdi:010064148},
}