Nitrogenase of Klebsiella pneumoniae. Rhodanese-catalysed restoration of activity of the inactive 2Fe species of the Fe protein.
The inactive 2Fe species of the Fe protein of the nitrogenase of Klebsiella pneumoniae was generated by treating oxidized Fe protein (Kp2) with MgATP and chelator. Incubation of the 2Fe species of Kp2 with the sulphurtransferase rhodanese in the presence of thiosulphate, ferric citrate and reduced lipoate reproducibly restored activity. The extent of restoration of activity depended on the molar ratio of 2Fe Kp2 to rhodanese and was time-dependent. Re-activation did not occur in the reaction mixture lacking rhodanese.
Pagani
S
S
A.F.R.C. Unit of Nitrogen Fixation, University of Sussex, Brighton, U.K.
Eldridge
M
M
Eady
R R
RR
D004789:Enzyme Activation / Q000187:drug effects; D007501:Iron / Q000378:metabolism; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D009591:Nitrogenase / Q000378:metabolism*; D013053:Spectrophotometry; D013466:Sulfurtransferases / Q000494:pharmacology*; D013884:Thiosulfate Sulfurtransferase / Q000494:pharmacology*
D007501:Iron; D009591:Nitrogenase; D013466:Sulfurtransferases; D013884:Thiosulfate Sulfurtransferase