1.19.6.1: nitrogenase (flavodoxin)
This is an abbreviated version!
For detailed information about nitrogenase (flavodoxin), go to the full flat file.
Word Map on EC 1.19.6.1
-
1.19.6.1
-
azotobacter
-
vinelandii
-
mgadp
-
mofe-protein
-
molybdenum-iron
-
nifu
-
rhodospirillum
-
dinitrogenase
-
femo-cofactor
-
pasteurianum
-
mgadp-bound
-
bacteriochlorophyll
-
nucleotide-bound
-
nitrogenases
-
dark-operative
-
nucleotide-induced
-
protochlorophyllide
-
agriculture
- 1.19.6.1
- azotobacter
- vinelandii
- mgadp
-
mofe-protein
-
molybdenum-iron
- nifu
-
rhodospirillum
- dinitrogenase
-
femo-cofactor
- pasteurianum
-
mgadp-bound
- bacteriochlorophyll
-
nucleotide-bound
- nitrogenases
-
dark-operative
-
nucleotide-induced
- protochlorophyllide
- agriculture
Reaction
4 reduced flavodoxin + 2 H+ + + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + + 16 ADP + 16 phosphate
Synonyms
FeP, FldA, NifF, nitrogenase, nitrogenase Fe protein, nitrogenase Fe-protein
ECTree
Advanced search results
Cofactor
Cofactor on EC 1.19.6.1 - nitrogenase (flavodoxin)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
FeMo protein
-
a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein, Fe6 within FeMo-cofactor provides the unique site for alkyne substrate binding and has van der Waals contact with the side chains of alpha-Val70l and alpha-Gln191, overview
-
MoFe protein
-
two parallel electron channels may exist between the [8Fe-7S] cluster and FeMo-cofactor
-
ATP
-
the Fe protein contains a single [4Fe-4S] cluster plus two MgATP binding sites
FeMo cofactor
-
structure, overview, a complex metallo-organic species called FeMo-cofactor provides the site of substrate reduction within the MoFe protein