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F388 A
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
F388H
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
F388T
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
F388Y
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197A
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197D
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197E
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197F
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197G
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197K
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197L
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site-directed mutagenesis, a variant of NifDDELTAH, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overviewup
H197N
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197Q
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197R
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197S
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197T
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197Y
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Q193A
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Q193G
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Q193H
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Q193K
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Q193L
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Q193N
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Q193S
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Q193V
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284C
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284E
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284F
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284H
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284K
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284L
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284Q
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284T
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
R284Y
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
S285A
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
S285C
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
S285D
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
S285G
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
S285M
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
S285N
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
S285Q
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
S285T
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Y236A
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Y236D
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Y236F
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Y236H
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Y236M
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Y236N
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
Y236T
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
H197A
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
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H197N
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
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H197T
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
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R284Q
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site-directed mutagenesis, a variant of NifDDELTAHup, nitrogen-fixing ability, H2 production rate, and reduction rate of acetylene (under Ar) of the mutant compared to the NifD control, overview
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A175G
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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
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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
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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
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alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, slightly decreased Fe protein activity, altered phenotype
H195L
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alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, increased Fe protein activity, altered phenotype
H195T
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alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein and Fe protein activity, altered phenotype
H195Y
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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
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site-directed mutagenesis, the double mutation does result in significant reduction of 2-butyne, with the exclusive product being 2-cis-butene
Q191K
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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
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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
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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
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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
V70A
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mutation in MoFe subunit. Mutant protein will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane
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V70G
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mutation in MoFe subunit. Mutant protein will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane
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R96Q
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the substitution of Arg to Gln at position 96 makes the active site pocket environment more hydrophobic than that of the native enzyme
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V70A
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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
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DELTAC153
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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
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S188C
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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
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H195N
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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
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alpha-His of MoFe protein, site directed mutagenesis, reduced MoFe protein activity, altered phenotype
H195Q
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below 2% N2 reducing activity remaining compared to wild-type due to less effective N2 binding
H195Q
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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
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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
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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
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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
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site-directed mutagenesis, increased the hydrazine reduction activity, reduced Km comapred to the wild-type enzyme
V70A
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site-directed mutagenesis, substitution of alpha-70Val by alanine results in an increased capacity for the reduction of the larger alkyne propyne
V70A
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mutation in MoFe subunit. Mutant protein will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane
V70G
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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
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mutation in MoFe subunit. Mutant protein will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane
V70I
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site-directed mutagenesis, decreased the hydrazine reduction activity
V70I
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site-directed mutagenesis, substitution by isoleucine at this position nearly eliminates the capacity for the reduction of acetylene
V70I
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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
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engineering of cyanobacterial strains for enhanced photobiological production of H2 in an aerobic, nitrogen-containing environment, overview
additional information
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engineering of cyanobacterial strains for enhanced photobiological production of H2 in an aerobic, nitrogen-containing environment, overview
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additional information
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reduction of nitrogenase activity in cells overexpressing PII protein participating in nif regulation is due to partial ADP-ribosylation of the Fe-protein under derepressing conditions and a reduction in the amount of Fe-protein. In cells overexpressing the PZ protein which negatively regulates ammonium transport the nitrogenase reactivation after an ammonium shock is delayed
additional information
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additional information
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natural nifB deletion mutant, MoFe protein without FeMo-cofactor and with small changes in the electronic properties of the [4Fe-4S] cluster
additional information
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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
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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
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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
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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
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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
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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
additional information
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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
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additional information
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transposon insertion mutants of several plasmids
additional information
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strains mutated in the nifX or orf1 genes show 90% or 50% reduction in nitrogenase activity under low levels of iron or molybdenum, respectively
additional information
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generation of a chimeric enzyme NifDK/NifB-co in which the active site iron-molybdenum cofactor is replaced by NifB-co. NifB is a S-adenosyl-L-methionine radical enzyme that functions in the synthesis of NifB-co, an early precursor to FeMo-cofactor. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3
additional information
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generation of a chimeric enzyme NifDK/NifB-co in which the active site iron-molybdenum cofactor is replaced by NifB-co. NifB is a S-adenosyl-L-methionine radical enzyme that functions in the synthesis of NifB-co, an early precursor to FeMo-cofactor. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3
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additional information
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construction of 2 mutants strain: 1 kanamycin-resistant with a deletion in NifHDK and 1 kanamycin, gentamycin, and molybdenum-resistant with double deletion in nif HDK and modABCD
additional information
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construction of 2 mutants strain: 1 kanamycin-resistant with a deletion in NifHDK and 1 kanamycin, gentamycin, and molybdenum-resistant with double deletion in nif HDK and modABCD
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