Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(VO4)3- + ?
(VO2)+ + ?
-
reduction of vanadium(V) by reduced Fe-protein of enzyme to vanadium(IV), which then probably binds to the nucleotide binding site in place of the Mg2+ which is normally present. The oxidized Fe-protein is unable to reduce vanadate
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
3,3-difluorocyclopropene + dithionite
propene + 2-fluoropropene + ?
-
-
major products providing evidence for reductive C-F bond cleavage. Synthesis of propene requires 6 e-/6 H+ and of 2-fluoropropene requires 4 e-/4 H+. In both products, C=C bond cleavage rather than C-C bond cleavage is involved. No selectivity is observed in formation of cis and trans isomers of 1,3-d2-2-fluoropropene, whereas cis-1,3-d2-propene is the predominant 1,3-d2-propene product, indicating that one of the bound reduction intermediates on the pathway to propene is constrained geometrically. Reduction requires both N2ase proteins MoFe and Fe protein, ATP, and an exogenous reductant such as dithionite. A reduction mechanism, consistent with hydride transfer as a key step, is discussed
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
acetylene + ?
ethylene + ?
acetylene + dithionite + H+ + ATP + H2O
ethylene + ?
-
-
-
?
CN- + europium(II) diethylenetriaminepentaacetate + H+
?
-
-
cofactor-deficient enzyme catalyzes formation of methane, ethane, ethene, propane, propene, butene, butane, pentene, pentane
-
?
CO + dithionite + H+
CH4 + C2H6 + C2H4 + C3H6 + C3H8 + ?
-
no substrate for wild-type
MoFe subunit mutants V70A and V70G will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane. The rates and ratios of hydrocarbon production from CO can be adjusted by changing the flux of electrons through nitrogenase, by substitution of other amino acids located near the FeMo-cofactor, or by changing the partial pressure of CO. Increasing the partial pressure of CO shifts the product ratio in favor of the longer chain alkanes and alkenes
-
?
CO + europium(II) diethylenetriaminepentaacetate + H+
?
-
-
cofactor-deficient enzyme catalyzes formation of methane, ethane, ethene, propane, propene
-
?
CS2 + ?
H2S + ?
slow turnover
-
-
?
diazene + ?
?
-
modified nitrogenase variant V70A/H195Q under turnover conditions using diazene, methyldiazene, or hydrazine as substrate traps a common S = 1/2 intermediate. Such samples also contain a common intermediate with FeMo-co in an integer-spin state having a ground-state non-Kramers doublet. This species, designated H, has NH2 bound to FeMo-co and corresponds to the penultimate intermediate of N2 hydrogenation, the state formed after the accumulation of seven electrons/protons and the release of the first NH3, the S = 1/2 species corresponds to the final intermediate in N2 reduction, the state formed after accumulation of eight electrons/protons, with NH3 still bound to FeMo-co prior to release and regeneration of resting-state FeMo-co
-
-
?
dithionite + H+ + N2 + ATP
?
dithionite + H+ + N2 + ATP + CO2
CO + CH4 + C2H6 + C3H6 + C3H8 + C4H8 + C4H10 + ?
-
-
-
-
?
flavodoxin hydroquinone + H+ + N2 + ATP + H2O
?
-
-
-
-
?
hydrazine + reduced ferredoxin
2 NH3 + oxidized ferredoxin
-
-
-
?
hydroxylamine + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
-
-
?
methyl isocyanide + ?
?
-
-
-
?
methyldiazene + ?
?
-
-
-
-
?
N2 + 10 H+ + 8 e- + 16 ATP
2 NH4+ + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
N2 + 4 reduced ferredoxin
hydrazine + 4 oxidized ferredoxin
-
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
N2 + 8 e- + 8 H+ + 16 ATP
2 NH3 + H2 + 16 ADP + 16 phosphate
nitrite + 4 reduced ferredoxin + 5 H+
hydroxylamine + H2O + 4 oxidized ferredoxin
-
-
-
?
nitrite + 7 H+ + 12 ATP
NH3 + 2 H2O + 12 ADP + 12 phosphate
overall reaction
-
-
?
nitrite + H+ + ATP + reduced ferredoxin
NH3 + 2 H2O + 12 ADP + 12 phosphate + oxidized ferredoxin
overall reaction
-
-
?
propargyl alcohol + ?
?
-
wild-type enzyme and V70A mutant MoFe protein-containing enzyme
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
reduced ferredoxin + H+ + N2O + ATP
oxidized ferredoxin + H2O + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
reduced ferredoxin + H+ + SCN- + ATP
oxidized ferredoxin + H2S + HCN + ADP + phosphate
-
-
-
?
Ti4+ + H+ + N2 + ATP
?
-
in vitro substrate
-
-
?
additional information
?
-
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
active site for acetylene reduction interacts not directly with N2 reduction
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
anaerobic atmosphere
reduction cycle continues until complete reduction of the substrate to ethane
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
intermediate is a flavodoxin hydroquinone
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
slow enzyme
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
1-propyne, 1-butyne and allene are reduced to the corresponding alkenes
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
Fe protein and MoFe protein are assumed to associate and dissociate to transfer a single electron to the substrates, termed Fe protein cycle, driven by MgATP hydrolysis, with the dissociation of the Fe protein-MoFe protein complex being the rate limiting step of the cycle
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
overall reaction
-
-
?
acetylene + ?
ethylene + ?
-
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
?
dithionite + H+ + N2 + ATP
?
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
-
SO2- being the actual nitrogenase reductant, reaction kinetics
-
-
?
hydrazine + ?
?
-
-
-
-
?
hydrazine + ?
?
-
high activity with the Val70 mutant enzyme, poor substrate for the wild-type enzyme
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
-
the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
-
relaxation of the nitrogenase H+/H+ intermediate during step-annealing
-
-
?
N2 + 8 e- + 8 H+ + 16 ATP
2 NH3 + H2 + 16 ADP + 16 phosphate
-
-
-
-
ir
N2 + 8 e- + 8 H+ + 16 ATP
2 NH3 + H2 + 16 ADP + 16 phosphate
-
cofactor binding structure analysis, Fe protein-MoFe protein complex structure in the presence of ATP analogue AMPPCP, overview
-
-
ir
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
enzyme complex is responsible for the majority of biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
in absence of N2 or other substrates, the electron flow is directed towards proton reduction
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
turnover cycle scheme, MgATP is required for activity, mechanism of MgATP hydrolysis and electron transfer with an important role of switch I and II within the Fe protein
-
-
ir
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
mutant H195Q shows only about 7.5% activity compared to wild-type
-
?
additional information
?
-
the activity of the enzyme complex is regulated by specific interactions, inducing conformational changes, between the complex components, overview
-
-
?
additional information
?
-
catalytic role of the molybdenum-iron protein, with P-cluster, and the Fe protein
-
-
?
additional information
?
-
-
nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth
-
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant enzymes, reduction reactions using acetylene, propyne, 1-butyne, 2-butyne, propargyl alcohol, 2-butyne-1-ol, and 2-butyne-1,4-diol as substrates, overview
-
-
?
additional information
?
-
-
nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor
-
-
?
additional information
?
-
substrates bind and are reduced at a single 4Fe-4S face of the FeMo-cofactor. When alpha70Val is substituted by alpha70Ile, access of substrates to Fe6 of this face is effectively blocked
-
-
?
additional information
?
-
-
in the draft mechanism model, H2 is produced by reductive elimination of the two bridging hydrides of a four-electron reduced intermediate during N2 binding. This process releases H2, yielding N2 bound to FeMo-cofactor that is doubly reduced relative to the resting redox level, and thereby is activated to promptly generate bound diazene. This mechanism predicts that during turnover under D2/N2, the reverse reaction of D2 with the N2-bound product of reductive elimination would generate a dideutero-four-electron reduced intermediate, which can relax with loss of HD to the state designated two-electron reduced intermediate, with a single deuteride bridge. The predicted two-electron reduced intermediate(D) and four-electron reduced intermediate(2D) states are established by intercepting them with the nonphysiological substrate acetylene to generate deuterated ethylenes. That gaseous H2/D2 can reduce a substrate other than H+ with N2 as a cocatalyst confirms the essential mechanistic role for H2 formation, and hence a limiting stoichiometry for biological nitrogen fixation of eight electrons/protons
-
-
?
additional information
?
-
-
a variant enzym containing P-clusters which consist of paired [Fe4S4]-like clusters, can catalyze ATP-independent substrate reduction in the presence of a strong reductant, europium (II) diethylenetriaminepentaacetate [Eu(II)-DTPA]. The variant P*-cluster is not only capable of catalyzing the two-electron reduction of proton, acetylene, ethylene, and hydrazine, but also capable of reducing cyanide, carbon monoxide, and carbon dioxide to alkanes and alkenes
-
-
?
additional information
?
-
-
data support a deficit-spending model of electron transfer where the first event is electron tranfer from the P-cluster to FeMo-cofactor and the second, backfill, event is fast electron tranfer from the Fe protein [4Fe-4S] cluster to the oxidized P-cluster. The first electron transfer is conformationally gated, whereas the second is not
-
-
?
additional information
?
-
-
draft mechanism for N2 reduction by nitrogenase. Diazene binds to the one-electron reduced intermediate with the release of H2, and enters the N2 pathway as the final form of the four-electron reduced state. In contrast, N2H4 instead binds to one-electron reduced intermediate, as is proposed for another two-electron substrate, C2H2, and joins the N2 pathway at a stage corresponding to the seven-electron reduced intermediate in the N2 reduction scheme
-
-
?
additional information
?
-
-
using buffer 3-(N-morpholino)propanesulfonic acid, which has a very small temperature coefficient, temperature-dependent elctron transfer rate constants are observed, with nonlinear Arrhenius plots and with electron transfers gated across the temperature range by a conformational change that involves the binding of numerous water molecules, consistent with an unchanging electron transfer mechanism. There is no solvent kinetic isotope effect throughout the temperature range studied, consistent with an unchanging mechanismn. The nonlinear Arrhenius plots are explained by the change in heat capacity caused by the binding of water molecules in an invariant gating electron transfer mechanism. The observations contradict the idea of a change in electron transfer mechanism with cooling
-
-
?
additional information
?
-
nitrite and hydroxylamine are nitrogenase substrates. The proposed NO2- reduction intermediate hydroxylamine (NH2OH) is a nitrogenase substrate, reduction intermediates can be trapped, cf. EC 1.7.2.2
-
-
?
additional information
?
-
nitrite and hydroxylamine as nitrogenase substrates. The proposed NO2- reduction intermediate hydroxylamine (NH2OH) is a nitrogenase substrate, reduction intermediates can be trapped, cf. EC 1.7.2.2
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe
-
molybdenum-iron protein component and an iron protein component with an iron-molybdenum cofactor center. Schematic structure of the alpha2-dimeric Fe protein, which contains a [Fe4S4] cluster at the subunit interface and an MgATP binding site within each subunit, overview
Mo
-
molybdenum-iron protein component with an iron-molybdenum cofactor center. Schematic structureof the alpha2beta2-tetrameric MoFe protein, which contains a pair of unique clusters in each ab-subunit dimer, the P-cluster ([Fe8S7]) at the alphabeta-subunit interface, and the FeMoco ([MoFe7S9X], where X=C,N, or O) within the alpha-subunit
Co2+
-
can replace Mg2+, but is less effective
Co2+
-
divalent cation requirement is satisfied by Co2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
Fe2+
-
Fe2+
-
can replace Mg2+, but is less effective
Fe2+
-
divalent cation requirement is satisfied by Fe2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
Fe2+
-
in [Fe-S] clusters
Fe2+
-
part of the iron-molybdenum and molybdenum-iron cofactors
Iron
-
-
Iron
-
enzyme consists of 2 proteins: a molybdenum and iron-containing protein, MoFe protein, component I, dinitrogenase, and an iron containing protein, Fe protein, component II, dinitrogenase reductase, together they form the active nitrogenase complex
Iron
-
iron content of MoFe protein: 30
Iron
-
the MoFe protein contains 2 molybdenum, about 30 iron and 30 inorganic sulphur atoms, 16 of the 30 Fe atoms are associated with S2- in four cubic [4Fe-4S] clusters, the remaining metal atoms are arranged in two copies of a cofactor called FeMo cofactor, FeMoCo, with a minimum stoichiometry of MoFe6S8-9
Iron
-
characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins
Iron
-
17-19 atoms of iron per molecule of MoFe protein, overview
Iron
-
4 atoms of iron per molecule of Fe protein
Iron
-
18-36 atoms of iron per molecule of MoFe protein , overview
Iron
-
VFe protein form 1 is an incomplete form that contains only 1 cofactor and 1 [4Fe-4S] cluster with an additional [Fe4-S4]-like cluster
Iron
-
reduction kinetics
Iron
-
contains [4Fe4S] cluster
Iron
-
dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site, the enzyme complex contains also a dimeric iron protein
Iron
dependent on, the enzyme complex contains a molybdenum-iron, a tetramer with 2 different subunits and 4 organo-metallic clusters, i.e. 2 iron-molybdenum cofactors and 2 P-clusters encoded by the genes nifD and nifK, the enzyme complex contains also a dimeric iron protein, encoded by the nifH gene, with a [4Fe4S] cluster between subunits and 2 MgATP binding sites, mechanism of electron transfer between metal clusters, mechanism of switch I and II, complex formation with the MoFe protein, also between different species, overview
Iron
-
enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, 1 of 2 different models proposes one or more Fe atoms in the Mo cofactor to be responsible for substrate binding
Iron
-
enzyme contains an iron-molybdenum cofactor
Iron
-
freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate in mutant V70A/H195Q. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor
Iron
in FeMo cofactor and MoFe protein
Iron
-
in the FeMo cofactor
Iron
-
in the MoFe protein and the Fe protein
Iron
contains iron and a Fe-Mo cofactor (the active site, a [7Fe:9S:Mo:C:R-homocitrate] cluster)
Mg2+
-
-
Mg2+
-
divalent metal requirement is satisfied by Mg2+, reaction is best supported by concentration of divalent cation one-half the concentration of ATP
Mg2+
-
Mg2+ required for MgATP complex
440138, 440144, 440145, 440146, 440147, 440158, 440166, 440174, 440175, 440178, 440180, 440182, 440184, 440186, 440187
Mg2+
required for ATP binding and MgATP hydrolysis, 2 MgATP binding sites on the iron protein connected via residues K15, D125, and C132, binding changes the conformation and the redox status of the [4Fe4S] cluster of the iron protein, mechanism, overview
Mg2+
-
MgATP2- is required
Mg2+
-
5 mM MgCl2 used in assay conditions
Mn2+
-
can replace Mg2+, but is less effective
Mn2+
-
divalent cation requirement is satisfied by Mn2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
Molybdenum
-
-
Molybdenum
contains molybdenum
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
characterization of the metal clusters in the nitrogenase molybdenum-iron protein
Molybdenum
-
review on molybdenum in nitrogenase
Molybdenum
-
molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview
Molybdenum
-
2 gatom per mol of MoFe protein
Molybdenum
-
also possesses Mo-independent nitrogenases: one vanadium containing nitrogenase and another lacking both molybdenum and vanadium
Molybdenum
-
enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex
Molybdenum
-
MoFe-cofactor contains 2 clusters of composition [4Fe-3S] and [1Mo-3Fe-3S] that are brigded by 3 nonprotein ligands
Molybdenum
-
mol Mo per mol MoFeprotein: wild-type and mutant H195Q 1.9, mutant H195N and Q191K 0.9
Molybdenum
-
dependent on, the enzyme complex contains a molybdenum-iron protein harboring the active site, the cofactor is composed of a [Mo-3Fe-3S] subcluster and a [4Fe3S] subcluster bridged by 3 sulfide pairs, with homocitrate bound to the molybdenum, structure determination and analysis
Molybdenum
dependent on, the enzyme complex contains a molybdenum-iron, a tetramer with 2 different subunits and 4 organo-metallic clusters, i.e. 2 iron-molybdenum cofactors [7Fe-Mo-9S-X-homocitrate] and 2 P-clusters [8Fe-7S], mechanism of electron transfer between metal clusters, complex formation with the Fe protein, also between different species, overview
Molybdenum
-
enzyme contains a [7Fe9S-Mo-X-homocitrate] metallocluster, where X can be an N atom, 1 of 2 different models proposes molydenum as the substrate binding partner in the active site
Molybdenum
-
enzyme contains an iron-molybdenum cofactor
Molybdenum
-
freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate in mutant V70A/H195Q. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor
Molybdenum
-
part of the iron-molybdenum and molybdenum-iron cofactors
Molybdenum
in FeMo cofactor and MoFe protein
Molybdenum
-
in the FeMo cofactor
Molybdenum
-
in the MoFe protein
Molybdenum
contains a Fe-Mo cofactor (the active site, a [7Fe:9S:Mo:C:R-homocitrate] cluster)
Ni2+
-
can replace Mg2+, but is less effective
Ni2+
-
divalent cation requirement is satisfied by Ni2+, is best supported by concentrations of divalent cation one-half the concentration of ATP
Vanadium
-
VFe protein form 1 is an incomplete form that contains only 1 cofactor and 1 [4Fe-4S] cluster with an additional [Fe4-S4]-like cluster
Vanadium
-
2 forms of VFe protein: form 1 has V-toFe ratio of 1:19, form 2 of 1:15
Vanadium
-
characterization of the metal clusters in the nitrogenase vanadium-iron protein
Vanadium
-
possesses 2 molybdenum-independent nitrogenases: one vanadium-containing nitrogenase and another lacking both molybdenum and vanadium
additional information
-
-
additional information
-
-
additional information
-
other metal ions, e.g. Cu2+, Mg2+, Zn2+, Ca2+, at levels of 1-2 atoms per mol detected in the MoFe protein, no evidence for specific requirement, except for Mg2+ in MgATP complex, of any of these metals
additional information
-
metal-sulfur cluster, e.g. [4Fe-4S]
additional information
-
structure and organization of metal clusters
additional information
-
structure and organization of metal clusters
additional information
-
structure and organization of metal clusters
additional information
structure catalytic role, and mechanism of the P-cluster, part of the MoFe protein, which has a role in immediate electron acceptance from the Fe protein
additional information
-
structures of the metal centers in Fe protein and MoFe protein, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A175G
-
shows in vivo 55% of enzyme activity compared to wild-type, in vitro 20% activity remaining with purified enzyme, slowlier conformational change upon binding of MgATP, model of steric interactions using x-ray crystal structures
A175S
-
unable to support substrate reduction because of an inability to undergo a required MgATP-induced conformational change
D125E
site-directed mutagenesis, mutation alters the properties of the MgATP2- binding site with bound MgADP
DELTAC153
-
mutation in the MoFe protein of nitrogenase. The rate of oxidation of Fe-protein F1+ to this MoFe protein variant is unchanged from the rate to the wild-type MoFe protein, providing further evidence against a gated hopping electron tansfer model
G69S
random mutagenesis, beta-subunit residue mutant of the MoFe protein shows highly decreased affinity for acetylene, acetylene inhibits the mutants nitrogen reduction activity in a competitive mode in contrast to the wild-type enzyme
H195G
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, slightly decreased Fe protein activity, altered phenotype
H195L
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, increased Fe protein activity, altered phenotype
H195T
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype
H195Y
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype
K15Q
site-directed mutagenesis, mutation inhibits the communication of the [4Fe4S] cluster with the MgATP2- binding site
Q191A/V70A
-
site-directed mutagenesis, the double mutation does result in significant reduction of 2-butyne, with the exclusive product being 2-cis-butene
Q191K
-
alphaGln191 of MoFe protein, shows 6% activity compared to wild-type, substrate CN-, not affected by addition of C2H2
R96Q
the substitution of Arg to Gln at position 96 makes the active site pocket environment more hydrophobic than that of the native enzyme
S69G
-
alpha-subunit MoFe protein, resistant to inhibition by C2H2, thus acetylene binding/reduction site is not directly relevant to the mechanism of nitrogen reduction
V70A/H195Q
-
mutant used for freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor. EPR and ENDOR analysis of the adduct
V70X
-
site-directed mutagenesis, substitution of valine with an amino acid with a smaller side chain increases the hydrazine reduction activity, substitution with an amino acid with a larger side chain decreases the enzyme activity with N2, acetylene or hydrazine
H195N
-
alphaHis195 of MoFe protein, shows 59% activity compared to wild-type, substrate CN-, NH3 and CH4 production from CN- are decreased by C2H2 addition, NH3 production decreased much less
H195N
-
alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, altered phenotype
H195Q
-
below 2% N2 reducing activity remaining compared to wild-type due to less effective N2 binding
H195Q
-
alphaHis195 of MoFe protein, shows 159% activity compared to wild-type, substrate CN-, NH3 and CH4 production from CN- are decreased by C2H2 addition
H195Q
-
alpha-His of MoFe protein, site directed mutagenesis, decreased MoFe protein activity, altered phenotype
H195Q
the mutant shows stronger nuclear resonance vibrational spectroscopy features in the Fe-CO region compared to wild type enzyme
S188C
site-directed mutagenesis, mutation of a residue within the P-cluster of the beta-subunit, alters the EPR signal of the MoFe protein
S188C
-
mutation in the MoFe protein of nitrogenase. Electron transfer to the MoFe state that contains P-cluster PN and FeMo-cofactor MN is conformationally gated in both wild-type MoFe and S188C mutant MoFe protein and the amino acid substitution S188C does not alter the conformational gate
V70A
-
site-directed mutagenesis of an alpha subunit residue of the MoFe cofactor, mutation alters the active site structure, trapping of propargyl alcohol at the active site for structure analysis
V70A
-
site-directed mutagenesis, increased the hydrazine reduction activity, reduced Km comapred to the wild-type enzyme
V70A
-
site-directed mutagenesis, substitution of alpha-70Val by alanine results in an increased capacity for the reduction of the larger alkyne propyne
V70A
-
mutation in MoFe subunit. Mutant protein will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane
V70G
-
site-directed mutagenesis, the mutant MoFe protein variant shows an increased capacity for reduction of the terminal alkyne, 1-butyne, but no detectable reduction of the internal alkyne 2-butyne
V70G
-
mutation in MoFe subunit. Mutant protein will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane
V70I
-
site-directed mutagenesis, decreased the hydrazine reduction activity
V70I
-
site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene
V70I
-
the mutant is suitable for analysis of reaction intermediates, since it exhibits the highest concentration of trapped H+-intermediate when turned over under Ar
V70I
substitution of alpha70Val by alpha70Ile results in a MoFe protein that is hampered in its ability to reduce a range of substrates including acetylene and N2, yet retains normal proton reduction activity. The mutant shows H2 evolution of greater than 2200 nmol/min/mg MoFe protein, which is 95% of the wild-type specific activity
additional information
-
-
additional information
-
natural nifB deletion mutant, MoFe protein without FeMo-cofactor and with small changes in the electronic properties of the [4Fe-4S] cluster
additional information
-
construction of mutant strain RP114
additional information
deletion of nifH results in an enzyme complex with a MoFe protein exhibiting altered redox properties and no EPR signal, a Fe protein Lys127 deletion mutant mimics the MgATP-bound-conformation and inhibits nucleotide hydrolyzing activity, formation of nondissociating complex with the MoFe protein
additional information
-
study of two nifB deletion mutants, having His-tagged MoFe/VFe protein, and two nifH deletion mutants, having His-tagged MoFe proteins, with catalytically active P-cluster variants presumably composed of [4Fe-4S]-like centers that are clearly distinct from the normal P-clusters. Proteins are active in terms of H2 evolution, C2H2 reduction, and N2 fixation upon FeMoco insertion
additional information
-
construction of mutant Azotobacter vinelandii strains DJ1242, DJ1313, and DJ1495, the mutant show loss of the ability to grow under nitrogen fixing conditions, phenotypes, overview
additional information
-
in vitro synthesis of the iron-molybdenum cofactor of nitrogenase using purified proteins, a minimal in vitro system, containing NifB, NifEN, and NifH proteins, together with Fe2+, S2-, MoO4 2-, R-homocitrate, S-adenosyl methionine, and Mg-ATP, is sufficient for the synthesis of FeMo-co and the activation of apo-dinitrogenase under anaerobic-reducing conditions, modeling, overview
additional information
-
a MoFeP variant labeled on its surface with a Ru-photosensitizer is shown to photocatalytically reduce protons and acetylene, most likely at its active site, FeMoco. The uncoupling of nitrogenase catalysis from ATP hydrolysis enables the study of redox dynamics within MoFeP and the population of discrete reaction intermediates, overview
additional information
-
a P-cluster variant, which consists of paired [Fe4S4]-like clusters, can catalyze ATP-independent substrate reduction in the presence of a strong reductant, europium (II) diethylenetriaminepentaacetate [Eu(II)-DTPA]. The observation of a decrease of activity in the rank DELTAnifH, DELTAnifB/DELTAnifZ, and DELTAnifB MoFe protein, corresponds to a decrease of the amount of variant P-clusters in these cofactor-deficient proteins and firmly establishes the variant P-cluster as a catalytically active metal center in Eu(II)-diethylenetriaminepentaacetate-driven reactions. The variant P-cluster is not only capable of catalyzing the two-electron reduction of proton, acetylene, ethylene, and hydrazine, but also capable of reducing cyanide, carbon monoxide, and carbon dioxide to alkanes and alkenes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Haaker, H.; Klugkist, J.
The bioenergetics of electron transport to nitrogenase
FEMS Microbiol. Rev.
46
57-71
1987
Azotobacter vinelandii, Anabaena cylindrica, Anabaena sp., Azospirillum sp., Azotobacter sp., Paenibacillus polymyxa, Chlorobium sp., Chromatium sp., Clostridium pasteurianum, Desulfovibrio sp., Frankia sp., Gloeothece sp., Klebsiella pneumoniae, Leptolyngbya boryana, Rhizobium leguminosarum, Rhizobium sp., Cereibacter sphaeroides, Rhodopseudomonas sp., Rhodospirillum rubrum, Rhizobium sp. ORS 571
-
brenda
Duyvis, M.G.; Wassink, H.; Haaker, H.
Nitrogenase of Azotobacter vinelandii: kinetic analysis of the Fe protein redox cycle
Biochemistry
37
17345-17354
1998
Azotobacter vinelandii
brenda
Vignais, P.M.; Colbeau, A.; Willison, J.C.; Jouanneau, Y.
Hydrogenase, nitrogenase, and hydrogen metabolism in the photosynthetic bacteria
Adv. Microb. Physiol.
26
155-234
1985
Azotobacter vinelandii, Allochromatium vinosum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhodobacter capsulatus, Rhodospirillum rubrum
brenda
Eady, R.R.
Isolation and characterization of various nitrogenases
Methods Enzymol.
69
753-778
1980
Azotobacter vinelandii, Allochromatium vinosum, Azotobacter chroococcum, Paenibacillus polymyxa, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Bradyrhizobium lupini, Rhodospirillum rubrum
-
brenda
Winter, H.C.; Burris, R.H.
Nitrogenase
Annu. Rev. Biochem.
45
409-426
1976
Azotobacter vinelandii, Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Paenibacillus polymyxa, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Klebsiella pneumoniae, Bradyrhizobium lupini, Rhodospirillum rubrum
brenda
Eady, R.R.; Postgate, J.R.
Nitrogenase
Nature
249
805-810
1974
Azotobacter vinelandii, Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Paenibacillus polymyxa, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Klebsiella pneumoniae, Ornithopus sativus, Leptolyngbya boryana, Bradyrhizobium lupini, Rhizobium sp., Rhodospirillum rubrum, Escherichia coli C-M 74, Corynebacterium flavescens 301
brenda
Mortenson, L.E.; Thorneley, R.N.F.
Structure and function of nitrogenase
Annu. Rev. Biochem.
48
387-418
1979
Azotobacter vinelandii, Azotobacter chroococcum, Paenibacillus polymyxa, Clostridium pasteurianum, Klebsiella pneumoniae
brenda
Shah, V.K.; Ugalde, R.A.; Imperial, J.; Brill, W.J.
Molybdenum in nitrogenase
Annu. Rev. Biochem.
53
231-257
1984
Azotobacter vinelandii, Paenibacillus polymyxa, Clostridium pasteurianum, Klebsiella pneumoniae
brenda
Pau, R.N.
Nitrogenases without molybdenum
Trends Biochem. Sci.
14
183-186
1989
Azotobacter vinelandii, Azotobacter chroococcum
brenda
Weininger, M.S.; Mortenson, L.E.
Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii
Proc. Natl. Acad. Sci. USA
79
379-380
1982
Azotobacter vinelandii, Clostridium pasteurianum
-
brenda
Burns, R.C.; Hardy, R.W.F.
Purification of nitrogenase and crystallization of its Mo-Fe protein
Methods Enzymol.
24
480-496
1972
Azotobacter vinelandii
brenda
Pau, R.N.; Mitchenall, L.A.; Robson, R.L.
Genetic evidence for an Azotobacter vinelandii nitrogenase lacking molybdenum and vanadium
J. Bacteriol.
171
124-129
1989
Azotobacter vinelandii
brenda
Morningstar, J.E.; Johnson, M.K.; Case, E.E.; Hales, B.J.
Characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins of Azotobacter vinelandii using magnetic circular dichroism spectroscopy
Biochemistry
26
1795-1800
1987
Azotobacter vinelandii
brenda
Bulen, W.A.; LeComte, J.R.
Nitrogenase complex and its components
Methods Enzymol.
24B
456-470
1972
Azotobacter vinelandii
brenda
Burgess, B.K.; Jacobs, D.B.; Stiefel, E.I.
Large-scale purification of high activity Azotobacter vinelandii nitrogenase
Biochim. Biophys. Acta
614
196-209
1980
Azotobacter vinelandii
brenda
Oelze, J.
Mechanismen zum Schutz der Sauerstoff-labilen Nitrogenase
Forum Mikrobiol.
4
116-126
1988
Azotobacter vinelandii, Anabaena sp., Trichormus variabilis, Azospirillum brasilense, Azotobacter chroococcum, Azotobacter sp., Frankia sp., Gloeothece sp., Klebsiella pneumoniae, Oscillatoria sp., Rhizobium sp., Rhodospirillum rubrum
-
brenda
Zumft, W.G.; Mortenson, L.E.
The nitrogen-fixing complex of bacteria
Biochim. Biophys. Acta
416
1-52
1975
Azotobacter vinelandii, Chromatium sp., Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium sp.
brenda
Duyvis, M.G.; Wassink, H.; Haaker, H.
Pre-steady-state MgATP-dependent proton production and electron transfer by nitrogenase from Azotobacter vinelandii
Eur. J. Biochem.
225
881-890
1994
Azotobacter vinelandii
brenda
Rasche, M.E.; Seefeldt, L.C.
Reduction of thiocyanate, cyanate, and carbon disulfide by nitrogenase: kinetic characterization and EPR spectroscopic analysis
Biochemistry
36
8574-8585
1997
Azotobacter vinelandii
brenda
Christiansen, J.; Goodwin, P.J.; Lanzilotta, W.N.; Seefeldt, L.C.; Dean, D.R.
Catalytic and biophysical properties of a nitrogenase Apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii
Biochemistry
37
12611-12623
1998
Azotobacter vinelandii
brenda
Erickson, J.A.; Nyborg, A.C.; Johnson, J.L.; Truscott, S.M.; Gunn, A.; Nordmeyer, F.R.; Watt, G.D.
Enhanced efficiency of ATP hydrolysis during nitrogenase catalysis utilizing reductants That form the all-ferrous redox state of the Fe protein
Biochemistry
38
14279-14285
1999
Azotobacter vinelandii, Clostridium pasteurianum, Azotobacter vinelandii OP
brenda
Fisher, K.; Dilworth, M.J.; Kim, C.H.; Newton, W.E.
Azotobacter vinelandii nitrogenases with substitutions in the FeMo-cofactor environment of the MoFe protein: effects of acetylene or ethylene on interactions with H+, HCN, and CN-
Biochemistry
39
10855-10865
2000
Azotobacter vinelandii
brenda
Bursey, E.H.; Burgess, B.K.
Characterization of a variant iron protein of nitrogenase that is impaired in its ability to adopt the MgATP-induced conformational change
J. Biol. Chem.
273
16927-16934
1998
Azotobacter vinelandii
brenda
Christiansen, J.; Cash, V.L.; Seefeldt, L.C.; Dean, D.R.
Isolation and characterization of an acetylene-resistant nitrogenase
J. Biol. Chem.
275
11459-11464
2000
Azotobacter vinelandii
brenda
Dilworth, M.J.; Fisher, K.; Kim, C.H.; Newton, W.E.
Effects on substrate reduction of substitution of histidine-195 by glutamine in the alpha-subunit of the MoFe protein of Azotobacter vinelandii nitrogenase
Biochemistry
37
17495-17505
1998
Azotobacter vinelandii
brenda
Kim, J.; Rees, D.C.
Nitrogenase and biological nitrogen fixation
Biochemistry
33
389-397
1994
Azotobacter vinelandii, Azotobacter chroococcum, Clostridium pasteurianum
brenda
Johnson, J.L.; Tolley, A.M.; Erickson, J.A.; Watt, G.D.
Steady-state kinetic studies of dithionite utilization, component protein interaction, and the formation of an oxidized iron protein intermediate during Azotobacter vinelandii nitrogenase catalysis
Biochemistry
35
11336-11342
1996
Azotobacter vinelandii
brenda
Blanchard, C.Z.; Hales, B.J.
Isolation of two forms of the nitrogenase VFe protein from Azotobacter vinelandii
Biochemistry
35
472-478
1996
Azotobacter vinelandii
brenda
Kim, C.H.; Newton, W.E.; Dean, D.R.
Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis
Biochemistry
34
2798-2808
1995
Azotobacter vinelandii
brenda
Benton, P.M.; Laryukhin, M.; Mayer, S.M.; Hoffman, B.M.; Dean, D.R.; Seefeldt, L.C.
Localization of a substrate binding site on the FeMo-cofactor in nitrogenase: trapping propargyl alcohol with an alpha-70-substituted MoFe protein
Biochemistry
42
9102-9109
2003
Azotobacter vinelandii, Azotobacter vinelandii DJ1310
brenda
Seefeldt, L.C.; Dance, I.G.; Dean, D.R.
Substrate interactions with nitrogenase: Fe versus Mo
Biochemistry
43
1401-1409
2004
Azotobacter vinelandii
brenda
Igarashi, R.Y.; Seefeldt, L.C.
Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase
Crit. Rev. Biochem. Mol. Biol.
38
351-384
2003
Azotobacter vinelandii (P00459)
brenda
Rubio, L.M.; Singer, S.W.; Ludden, P.W.
Purification and characterization of NafY (apodinitrogenase gamma subunit) from Azotobacter vinelandii
J. Biol. Chem.
279
19739-19746
2004
Azotobacter vinelandii, Azotobacter vinelandii DJ
brenda
Barney, B.M.; Igarashi, R.Y.; Dos Santos, P.C.; Dean, D.R.; Seefeldt, L.C.
Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis
J. Biol. Chem.
279
53621-53624
2004
Azotobacter vinelandii
brenda
Barney, B.M.; Laryukhin, M.; Igarashi, R.Y.; Lee, H.I.; Dos Santos, P.C.; Yang, T.C.; Hoffman, B.M.; Dean, D.R.; Seefeldt, L.C.
Trapping a hydrazine reduction intermediate on the nitrogenase active site
Biochemistry
44
8030-8037
2005
Azotobacter vinelandii
brenda
Fisher, K.; Lowe, D.J.; Petersen, J.
Vanadium (V) is reduced by the 'as isolated' nitrogenase Fe-protein at neutral pH
Chem. Commun. (Camb. )
2006
2807-2809
2006
Azotobacter vinelandii
brenda
Dance, I.
The hydrogen chemistry of the FeMo-co active site of nitrogenase
J. Am. Chem. Soc.
127
10925-10942
2005
Azotobacter vinelandii
brenda
Lee, H.I.; Sorlie, M.; Christiansen, J.; Yang, T.C.; Shao, J.; Dean, D.R.; Hales, B.J.; Hoffman, B.M.
Electron inventory, kinetic assignment (E(n)), structure, and bonding of nitrogenase turnover intermediates with C2H2 and CO
J. Am. Chem. Soc.
127
15880-15890
2005
Azotobacter vinelandii
brenda
Dance, I.
The mechanistically significant coordination chemistry of dinitrogen at FeMo-co, the catalytic site of nitrogenase
J. Am. Chem. Soc.
129
1076-1088
2007
Azotobacter vinelandii
brenda
Hu, Y.; Corbett, M.C.; Fay, A.W.; Webber, J.A.; Hedman, B.; Hodgson, K.O.; Ribbe, M.W.
Nitrogenase reactivity with P-cluster variants
Proc. Natl. Acad. Sci. USA
102
13825-13830
2005
Azotobacter vinelandii
brenda
Dos Santos, P.C.; Mayer, S.M.; Barney, B.M.; Seefeldt, L.C.; Dean, D.R.
Alkyne substrate interaction within the nitrogenase MoFe protein
J. Inorg. Biochem.
101
1642-1648
2007
Azotobacter vinelandii, Azotobacter vinelandii DJ995
brenda
Curatti, L.; Hernandez, J.A.; Igarashi, R.Y.; Soboh, B.; Zhao, D.; Rubio, L.M.
In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins
Proc. Natl. Acad. Sci. USA
104
17626-17631
2007
Azotobacter vinelandii
brenda
Hu, Y.; Fay, A.W.; Lee, C.C.; Wiig, J.A.; Ribbe, M.W.
Dual functions of NifEN: insights into the evolution and mechanism of nitrogenase
Dalton Trans.
39
2964-2971
2010
Azotobacter vinelandii
brenda
Roth, L.E.; Nguyen, J.C.; Tezcan, F.A.
ATP- and iron-protein-independent activation of nitrogenase catalysis by light
J. Am. Chem. Soc.
132
13672-13674
2010
Azotobacter vinelandii
brenda
Sarma, R.; Barney, B.; Keable, S.; Dean, D.; Seefeldt, L.; Peters, J.
Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha70Ile MoFe protein variant
J. Inorg. Biochem.
104
385-389
2010
Azotobacter vinelandii (P07328)
brenda
Lee, C.C.; Hu, Y.; Ribbe, M.W.
Vanadium nitrogenase reduces CO
Science
329
642
2010
Azotobacter vinelandii
brenda
Kaiser, J.T.; Hu, Y.; Wiig, J.A.; Rees, D.C.; Ribbe, M.W.
Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase
Science
331
91-94
2011
Azotobacter vinelandii
brenda
Danyal, K.; Dean, D.R.; Hoffman, B.M.; Seefeldt, L.C.
Electron transfer within nitrogenase: evidence for a deficit-spending mechanism
Biochemistry
50
9255-9263
2011
Azotobacter vinelandii, Azotobacter vinelandii DJ995
brenda
Mayweather, D.; Danyal, K.; Dean, D.R.; Seefeldt, L.C.; Hoffman, B.M.
Temperature invariance of the nitrogenase electron transfer mechanism
Biochemistry
51
8391-8398
2012
Azotobacter vinelandii, Azotobacter vinelandii DJ995
brenda
Ni, F.; Lee, C.C.; Hwang, C.S.; Hu, Y.; Ribbe, M.W.; McKenna, C.E.
Reduction of fluorinated cyclopropene by nitrogenase
J. Am. Chem. Soc.
135
10346-10352
2013
Azotobacter vinelandii, Azotobacter vinelandii OP
brenda
Yang, Z.Y.; Dean, D.R.; Seefeldt, L.C.
Molybdenum nitrogenase catalyzes the reduction and coupling of CO to form hydrocarbons
J. Biol. Chem.
286
19417-19421
2011
Azotobacter vinelandii, Azotobacter vinelandii DJ1260
brenda
Wiig, J.A.; Hu, Y.; Ribbe, M.W.
NifEN-B complex of Azotobacter vinelandii is fully functional in nitrogenase FeMo cofactor assembly
Proc. Natl. Acad. Sci. USA
108
8623-8627
2011
Azotobacter vinelandii
brenda
Lukoyanov, D.; Yang, Z.Y.; Barney, B.M.; Dean, D.R.; Seefeldt, L.C.; Hoffman, B.M.
Unification of reaction pathway and kinetic scheme for N2 reduction catalyzed by nitrogenase
Proc. Natl. Acad. Sci. USA
109
5583-5587
2012
Azotobacter vinelandii, Azotobacter vinelandii DJ1260
brenda
Lee, C.C.; Hu, Y.; Ribbe, M.W.
ATP-independent substrate reduction by nitrogenase P-cluster variant
Proc. Natl. Acad. Sci. USA
109
6922-6926
2012
Azotobacter vinelandii, Azotobacter vinelandii DJ1143
brenda
Yang, Z.Y.; Khadka, N.; Lukoyanov, D.; Hoffman, B.M.; Dean, D.R.; Seefeldt, L.C.
On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase
Proc. Natl. Acad. Sci. USA
110
16327-16332
2013
Azotobacter vinelandii, Azotobacter vinelandii DJ1260
brenda
Shaw, S.; Lukoyanov, D.; Danyal, K.; Dean, D.R.; Hoffman, B.M.; Seefeldt, L.C.
Nitrite and hydroxylamine as nitrogenase substrates mechanistic implications for the pathway of N2 reduction
J. Am. Chem. Soc.
136
12776-12783
2014
Azotobacter vinelandii (P00459)
brenda
Yang, K.Y.; Haynes, C.A.; Spatzal, T.; Rees, D.C.; Howard, J.B.
Turnover-dependent inactivation of the nitrogenase MoFe-protein at high pH
Biochemistry
53
333-343
2014
Azotobacter vinelandii (P07328)
brenda
Morrison, C.N.; Hoy, J.A.; Zhang, L.; Einsle, O.; Rees, D.C.
Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites
Biochemistry
54
2052-2060
2015
Klebsiella pneumoniae (P00466 and P09772), Klebsiella pneumoniae, Clostridium pasteurianum (P00467 and P11347), Clostridium pasteurianum, Azotobacter vinelandii (P07328 and P07329), Azotobacter vinelandii
brenda
Sickerman, N.S.; Hu, Y.; Ribbe, M.W.
Activation of CO2 by vanadium nitrogenase
Chem. Asian J.
12
1985-1996
2017
Azotobacter vinelandii
brenda
Spatzal, T.; Perez, K.A.; Howard, J.B.; Rees, D.C.
Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor
eLife
4
e11620
2015
Azotobacter vinelandii
brenda
Buren, S.; Rubio, L.M.
State of the art in eukaryotic nitrogenase engineering
FEMS Microbiol. Lett.
365
2018
2018
Azotobacter vinelandii
brenda
Scott, A.D.; Pelmenschikov, V.; Guo, Y.; Yan, L.; Wang, H.; George, S.J.; Dapper, C.H.; Newton, W.E.; Yoda, Y.; Tanaka, Y.; Cramer, S.P.
Structural characterization of CO-inhibited Mo-nitrogenase by combined application of nuclear resonance vibrational spectroscopy, extended X-ray absorption fine structure, and density functional theory new insights into the effects of CO binding and the
J. Am. Chem. Soc.
136
15942-15954
2014
Azotobacter vinelandii (P07328 and P07329), Azotobacter vinelandii
brenda
Lukoyanov, D.; Yang, Z.Y.; Khadka, N.; Dean, D.R.; Seefeldt, L.C.; Hoffman, B.M.
Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N2 for H2
J. Am. Chem. Soc.
137
3610-3615
2015
Azotobacter vinelandii, Azotobacter vinelandii DJ995
brenda
Morrison, C.N.; Spatzal, T.; Rees, D.C.
Reversible protonated resting state of the nitrogenase active site
J. Am. Chem. Soc.
139
10856-10862
2017
Azotobacter vinelandii, Clostridium pasteurianum
brenda
Hu, Y.; Ribbe, M.W.
A journey into the active center of nitrogenase
J. Biol. Inorg. Chem.
19
731-736
2014
Azotobacter vinelandii, Clostridium pasteurianum
brenda
Dance, I.
New insights into the reaction capabilities of His195 adjacent to the active site of nitrogenase
J. Inorg. Biochem.
169
32-43
2017
Azotobacter vinelandii (P07328 and P07329)
brenda
Keable, S.; Vertemara, J.; Zadvornyy, O.; Eilers, B.; Danyal, K.; Rasmussen, A.; De Gioia, L.; Zampella, G.; Seefeldt, L.; Peters, J.
Structural characterization of the nitrogenase molybdenum-iron protein with the substrate acetylene trapped near the active site
J. Inorg. Biochem.
180
129-134
2018
Azotobacter vinelandii (P07328 and P07329), Azotobacter vinelandii DJ1264 (P07328 and P07329)
brenda
Rebelein, J.G.; Stiebritz, M.T.; Lee, C.C.; Hu, Y.
Activation and reduction of carbon dioxide by nitrogenase iron proteins
Nat. Chem. Biol.
13
147-149
2017
Azotobacter vinelandii
brenda
Ivleva, N.B.; Groat, J.; Staub, J.M.; Stephens, M.
Expression of active subunit of nitrogenase via integration into plant organelle genome
PLoS ONE
11
e0160951
2016
Azotobacter vinelandii
brenda
Fay, A.W.; Wiig, J.A.; Lee, C.C.; Hu, Y.
Identification and characterization of functional homologs of nitrogenase cofactor biosynthesis protein NifB from methanogens
Proc. Natl. Acad. Sci. USA
112
14829-14833
2015
Azotobacter vinelandii
brenda
Spatzal, T.; Perez, K.A.; Einsle, O.; Howard, J.B.; Rees, D.C.
Ligand binding to the FeMo-cofactor structures of CO-bound and reactivated nitrogenase
Science
345
1620-1623
2014
Azotobacter vinelandii
brenda