Open AccessThermal properties and oxygenase activity of ribulose‐1,5‐bisphosphate carboxylase from the thermophilic purple bacterium, Chromatium tepidum
Author(s) -
Heda Ghanshyam D.,
Madigan Michael T.
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb02966.x
Subject(s) - thermophile , chromatium , oxygenase , ribulose 1,5 bisphosphate , pyruvate carboxylase , biochemistry , ribulose , obligate anaerobe , bacteria , chemistry , biology , mesophile , rubisco , enzyme , photosynthesis , genetics
Ribulose‐1,5‐biphosphate carboxylase (RuBPCase) partially purified from the thermophilic purple bacterium Chromatium tepidum displayed maximum carboxylase activity at 50°C, while enzyme from a related mesophilic species, Chromatium vinosum , was completely inactive at 50°C. RuBPCase from C. tepidum showed ribulose‐1,5‐ bisphosphate‐dependent oxygenase activity, and, in addition, O 2 was found to partially destroy carboxylase activity. It is concluded that thermophilic purple bacteria produce heat‐stable RuBPCase and that all RuBPCases, even those from an obligate anaerobe such as C. tepidum , have associated oxygenase activity.