
Physiological characterisation of an Azotobacter vinelandii nifU ‐deletion mutant and its spontaneous Nif + revertants that over‐produce cytochrome bd
Author(s) -
Hill Susan,
He Luhong,
Kennedy Christina
Publication year - 1999
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.1574-6968.1999.tb13618.x
Subject(s) - azotobacter vinelandii , mutant , nitrogenase , cytochrome , mutation , chemistry , microbiology and biotechnology , biology , biochemistry , enzyme , genetics , gene , bacteria , nitrogen fixation
A nifU ‐deletion mutant of Azotobacter vinelandii fixed N 2 , but only under low atmospheric O 2 (2 kPa), whereas, under air, it reverted to Nif + at 5×10 −8 . The revertant's O 2 ‐tolerant nitrogenase activity, surprisingly, was not accompanied by an increased respiration rate, although, like cydR mutants, the revertants over‐produce cytochrome bd . The introduction of a cydR mutation into the nifU mutant yielded transformants, of which 100% fixed N 2 in air. This is consistent with the revertant mutations residing in cydR . Inactivation of CydR (a Fnr‐like transcriptional repressor) could lead to the up‐regulation of a process (e.g. IscU activity in i ron‐ s ulfur c luster formation) that substitutes for NifU.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom