Open Access8‐Hydroxy‐5‐deazaflavin‐dependent electron transfer in the extreme halophile Halobacterium cutirubrum
Author(s) -
Wit L.E.A.,
Eker A.P.M.
Publication year - 1987
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.1574-6968.1987.tb02527.x
Subject(s) - halobacterium , halophile , biology , oxidoreductase , halobacterium salinarum , electron transfer , biochemistry , chemistry , bacteria , archaea , enzyme , genetics , gene , photochemistry
Cell extracts of the extreme halophile Halobacterium cutirubrum were found to contain 8‐hydroxy‐5‐deazaflavin as well as 8‐OH‐5‐deazaflavin: NADPH oxidoreductase activity. The oxidoreductase was partially purified and showed maximum activity at pH 5.4, which is unusually low for halobacteria, and 5.3 M NaCl, close to the intracellular salt concentration. The results indicate the presence of an 8‐OH‐5‐deazaflavin‐dependent electron transfer system in a nonmethanogenic organism.