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Ferredoxin
physiological cofactor
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flavin
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flavin-dependent enzyme
FAD
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FAD
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non covalently bound
FAD
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flavoprotein with non-covalently bound FAD
FAD
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each subunit contains noncovalently bound FAD
FAD
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enzyme-bound FAD as coenzyme
FAD
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enzyme activity depends on the concentration of its cofactor FAD: maximum activity at 0.05 mM FAD
FAD
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flavoprotein with FAD as cofactor
FAD
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flavoprotein with FAD as cofactor
FAD
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FAD is essential for electron transfer between NADH and methylenetetrahydrofolate
FAD
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1.7 molecules enzyme-bound FAD per enzyme molecule
FAD
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flavoprotein, oxidized acceptor in reverse reaction
FAD
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flavoprotein, oxidized acceptor in reverse reaction
FAD
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flavoprotein, oxidized acceptor in reverse reaction
FAD
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flavoprotein, oxidized acceptor in reverse reaction
FAD
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requires FAD as cofactor
FAD
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redox properties of enzyme-bound FAD are influenced by Asp120, which electrostatically stabilizes putative 5-iminium cation intermediate during catalysis
FAD
the enzyme contains one FAD prosthetic group bound per dimer. Km for FAD is 0.005 mM. The enzyme activity of the FAD-replete enzyme is approximately 50% compared to the normal purified enzyme
FADH2
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FADH2
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flavoprotein, reduced acceptor in forward reaction
FADH2
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flavoprotein, reduced acceptor in forward reaction
FADH2
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flavoprotein, reduced acceptor in forward reaction
FADH2
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flavoprotein, reduced acceptor in forward reaction
FMN
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no effect
FMN
the enzyme contains 1.87 mol FMN per mol dimeric heterodimer. MetF binds the flavin
heme
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the diheme cytochrome NsapB constitutes the small subunit of the nitrate reductase. The two heme groups have nearly parallel heme planes. van der Waals distances with an iron-to-iron distance of 9.9 A. The two propionate side chaind on both heme groups are hydrogen-bonded to each other. The propionates of one of the heme groups are pulled towards the interior of the molecule due to a salt bridge and a number of hydrogen bonds between the propionates and conserved residues
heme
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the diheme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. The plasticity of the complex contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA
NAD+
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NAD+
only active with the chimeric mutant enzyme, not with the wild-type
NAD+
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recombinant wild-type and chimeric mutant enzymes
NADH
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NADH
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strong preference of NADH over NADPH as reductant
NADH
strong preference of NADH over NADPH as reductant
NADH
only active with the chimeric mutant enzyme, not with the wild-type
NADH
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recombinant wild-type and chimeric mutant enzymes
NADH
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dual-cofactor specificity with NADH and NADPH under physiological conditions
NADP+
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NADP+
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poor cofactor for the recombinant wild-type enzyme, but utilized by the chimeric mutant enzyme with activity equal to the activity with NAD+
NADPH
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NADPH
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NADPH-dependent reduction of methylenetetrahydrofolate, NADPH irreversibly reduces the enzyme-bound flavin
NADPH
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poor cofactor for the recombinant wild-type enzyme, but utilized by the chimeric mutant enzyme with activity equal to the activity with NADH
NADPH
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dual-cofactor specificity with NADH and NADPH under physiological conditions
NADPH
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the optimum concentration is 1.2 mM
additional information
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no direct activity with pyridine nucleotides: NADH, NADPH
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additional information
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no direct activity with pyridine nucleotides: NADH, NADPH
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additional information
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no direct activity with pyridine nucleotides: NADH, NADPH
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additional information
wild-type shows no activity with NADH/NAD+
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additional information
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wild-type shows no activity with NADH/NAD+
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additional information
FAD is not required, NADPH is highly preferred before NADH
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additional information
NADH and NADPH are not used as electron donor, but reduced ferredoxin is. The enzyme possesses two predicted 4Fe-4S-clusters in MetV
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