@article{fdi:010053554,
  title = {{O}xygen uptake rates in the hyperthermophilic anaerobe {T}hermotoga maritima grown in a bioreactor under controlled oxygen exposure : clues to its defence strategy against oxidative stress},
  author = {{L}akhal, {R}aja and {A}uria, {R}ichard and {D}avidson, {S}ylvain and {O}llivier, {B}ernard and {D}urand, {M}. {C}. and {D}olla, {A}. and {H}amdi, {M}. and {C}ombet-{B}lanc, {Y}annick},
  editor = {},
  language = {{ENG}},
  abstract = {{A} 2.3-{L} bioreactor was specially adapted to grow hyperthermophilic microorganisms under controlled conditions of temperature, p{H}, redox potential and dissolved {O}-2. {U}sing this bioreactor regulated at 80{A} degrees {C} and p{H} 7.0, we demonstrated that {T}hermotoga maritima recovered its growth despite being exposed to oxygen for a short time (30 min with a maximum concentration of 23 mu {M} of dissolved oxygen). {U}nder these conditions, we demonstrated that {O}-2 uptake rate, estimated at 73.6 mu moles {O}-2 min(-1) g proteins(-1) for dissolved oxygen, was optimal and constant, when dissolved oxygen was present in a range of 22-5 mu {M}. {T}ranscription analyses revealed that during short oxygen exposure, {T}. maritima expressed genes coding for enzymes to deal with {O}-2 and reactive oxygen species ({ROS}) such as peroxides. {T}hus, genes encoding {ROS}-scavenging systems, alkyl hydroperoxide reductase (ahp), thioredoxin-dependent thiol peroxidase (bcp 2) and to a lesser extent neelaredoxin (nlr) and rubrerythrin (rbr), were found to be upregulated during oxygen exposure. {T}he oxygen reductase {F}pr{A}, homologous to the rubredoxin-oxygen oxidoreductase ({ROO}) found in {D}esulfovibrio species, is proposed as a primary consumer of {O}-2 in {T}. maritima. {M}oreover, the expression of frp{A} was shown to depend on the redox ({E}h) level of the culture medium.},
  keywords = {{T}hermotoga maritima ; {O}xidative stress ; {O}xygen},
  booktitle = {},
  journal = {{A}rchives of {M}icrobiology},
  volume = {193},
  numero = {6},
  pages = {429--438},
  ISSN = {0302-8933},
  year = {2011},
  DOI = {10.1007/s00203-011-0687-8},
  URL = {https://www.documentation.ird.fr/hor/fdi:010053554},
}