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pro vyhledávání: '"Patrick Rühl"'
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
Persulfide dioxygenases (PDOs) are abundant in Bacteria and also crucial for H2S detoxification in mitochondria. One of the two pdo-genes of the acidophilic bacterium Acidithiobacillus caldus was expressed in Escherichia coli. The protein (AcPDO) had
Externí odkaz:
https://doaj.org/article/4ea2e96d452e4300802d7f67e3332020
Autor:
Patrick Rühl, Arnulf Kletzin
Publikováno v:
Bio-Protocol, Vol 7, Iss 14 (2017)
The sulfur oxygenase reductase (SOR) reaction is a dioxygen-dependent disproportionation of elemental sulfur (S0), catalyzed at optimal temperatures between 65 °C and 85 °C. Thiosulfate and sulfite are formed as oxidized products as well hydrogen s
Externí odkaz:
https://doaj.org/article/0ee49534e951413a9b10d214ce6a0133
Publikováno v:
Frontiers in Microbiology
Persulfide dioxygenases (PDOs) are abundant in Bacteria and also crucial for H2S detoxification in mitochondria. One of the two pdo-genes of the acidophilic bacterium Acidithiobacillus caldus was expressed in Escherichia coli. The protein (AcPDO) had
Publikováno v:
Journal of Bacteriology. 199
Sequence comparisons showed that the sulfur oxygenase reductase (SOR) of the haloalkaliphilic bacterium Thioalkalivibrio paradoxus Arh 1 ( Tp SOR) is branching deeply within dendrograms of these proteins (29 to 34% identity). A synthetic gene encodin
Autor:
Arnulf Kletzin, Patrick Rühl
Publikováno v:
Bio Protoc
The sulfur oxygenase reductase (SOR) reaction is a dioxygen-dependent disproportionation of elemental sulfur (S(0)), catalyzed at optimal temperatures between 65 °C and 85 °C. Thiosulfate and sulfite are formed as oxidized products as well hydrogen