Open AccessExpression and characterization of the terminal heme synthetic enzymes from the hyperthermophile Aquifex aeolicus
Author(s) -
Wang KaiFen,
Dailey Tamara A.,
Dailey Harry A.
Publication year - 2001
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.1574-6968.2001.tb10789.x
Subject(s) - aquifex aeolicus , heme , terminal (telecommunication) , enzyme , biochemistry , chemistry , biology , gene , escherichia coli , computer science , telecommunications
The terminal two heme biosynthetic pathway enzymes, protoporphyrinogen oxidase and ferrochelatase, of the hyperthermophilic bacterium Aquifex aeolicus have been expressed in Escherichia coli , purified to homogeneity, and biochemically characterized. Ferrochelatase and protoporphyrinogen oxidase of this organism are both monomeric, as was found for the corresponding enzymes of Bacillus subtilis . However, unlike the B. subtilis proteins, both A. aeolicus enzymes are membrane‐associated. Both proteins have temperature optima over 60°C. This is the first demonstration of functional heme biosynthetic enzymes in an extreme thermophilic bacterium.