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benzyl viologen-nitrate reductase
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EC 1.7.99.4
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formerly, part transferred
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nitrate reductase, periplasmic
periplasmic nitrate reductase
periplasmic nitrate reductases
reductase, nitrate (cytochrome)
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respiratory nitrate reductase
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single subunit Nap-type periplasmic nitrate reductase
additional information
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the enzymes EC 1.7.99.4 and EC 1.9.6.1 are probably identical, in vivo cytochrome serves as electron donor in the electron transport chain to nitrate
mmol_1648

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NAP

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Nap-alpha

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isoform
NAP-beta

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isoform
NapA

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NapA
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catalytic subunit of the periplasmic nitrate reductase system
NapAB

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NapABC

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NapDAGHB

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isoform
NapEDABC

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nitrate reductase, periplasmic

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nitrate reductase, periplasmic
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periplasmic nitrate reductase

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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductase
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periplasmic nitrate reductases

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periplasmic nitrate reductases
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periplasmic nitrate reductases
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periplasmic nitrate reductases
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single subunit Nap-type periplasmic nitrate reductase

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single subunit Nap-type periplasmic nitrate reductase
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O

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2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
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2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
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2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
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2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism. The second sphere type of mechanism is supported by the recent X-ray structures of Nap from Desulfovibrio desulf uricans ATCC 27774 and Cupriavidus necator H16, in which the sixth sulfur ligand of the Mo interacts with the sulfur from the cysteine residue and generates a bidentate persulfido ligand that sterically blocks the access of the substrate to the Mo ion, modelling
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
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2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
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2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
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2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
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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.
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
2 reduced methyl viologen + 2 H+ + nitrate
2 oxidized methyl viologen + nitrite
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
nitrate + reduced acceptor
nitrite + acceptor
nitrate + reduced acceptor
nitrite + oxidized acceptor
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nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen
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nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
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nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
nitrite + methyl viologen
nitrate + oxidized methyl viologen
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additional information
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2 ferrocytochrome + 2 H+ + nitrate

2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
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2 reduced methyl viologen + 2 H+ + nitrate

2 oxidized methyl viologen + nitrite
artificial electron acceptor
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r
2 reduced methyl viologen + 2 H+ + nitrate
2 oxidized methyl viologen + nitrite
artificial electron acceptor
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r
nitrate + ferrocytochrome

nitrite + ferricytochrome + H2O
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the periplasmic cytochrome c-linked nitrate reductase is encoded by the napFDAGHBC operon. The napF operon apparently encodes a low-substrate-induced reductase that is maximally expressed only at low levels of nitrate. Expression is suppressed under high-nitrate conditions. In contrast, the narGHJI operon is only weakly expressed at low nitrate levels but is maximally expressed when nitrate is elevated. The narGHJI operon is therefore a high-substrate-induced operon that somehow provides a second and distinct role in nitrate metabolism by the cell. Nitrite, the end product of each enzyme, has only a minor effect on the expression of either operon. Finally, nitrate, but not nitrite, is essential for repression of napF gene expression. These studies reveal that nitrate rather than nitrite is the primary signal that controls the expression of these two nitrate reductase operons in a differential and complementary fashion
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nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC
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nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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periplasmic nitrate reductase is expressed under nitrate-limiting conditions. NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via cytochrome NapC and NapB to NapA
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nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinoneubiquinol couple via cytochrome NapC and NapB to NapA
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nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB
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nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
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the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
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