1.9.6.1: nitrate reductase (cytochrome)
This is an abbreviated version!
For detailed information about nitrate reductase (cytochrome), go to the full flat file.
Word Map on EC 1.9.6.1
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1.9.6.1
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nitrite
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denitrification
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denitrify
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molybdenum
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paracoccus
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dissimilatory
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denitrificans
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n2o
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pantotrophus
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napf
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nitrate-reducing
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desulfuricans
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molybdoenzymes
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thiosphaera
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cyma
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fixk2
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menaquinol
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di-haem
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bismolybdopterin
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wolinella
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high-g
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narghi
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norcbqd
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nitrate-dependent
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mo-containing
- 1.9.6.1
- nitrite
-
denitrification
-
denitrify
- molybdenum
- paracoccus
-
dissimilatory
- denitrificans
- n2o
- pantotrophus
- napf
-
nitrate-reducing
- desulfuricans
-
molybdoenzymes
-
thiosphaera
-
cyma
- fixk2
- menaquinol
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di-haem
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bismolybdopterin
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wolinella
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high-g
- narghi
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norcbqd
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nitrate-dependent
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mo-containing
Reaction
2 ferrocytochrome + 2 H+ + = 2 ferricytochrome + +
Synonyms
benzyl viologen-nitrate reductase, EC 1.7.99.4, mmol_1648, More, NAP, NAP enzyme, Nap-alpha, NAP-beta, NapA, napA-beta, NapAB, NapABC, NapDAGHB, NapEDABC, nitrate reductase, periplasmic, periplasmic nitrate reductase, periplasmic nitrate reductases, reductase, nitrate (cytochrome), respiratory nitrate reductase, single subunit Nap-type periplasmic nitrate reductase
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Cofactor
Cofactor on EC 1.9.6.1 - nitrate reductase (cytochrome)
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cytochrome c552
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the enzyme is a complex of a 93000 Da polypeptide and a 16000 Da nitrate-oxidizable cytochrome c552, cytochrome c552 contains two c-type heme moieties
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
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the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
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NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
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subunit NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster
cytochrome
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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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cytochrome
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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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cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
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contains 1.3 mol heme per mol of protein (assuminga 110-kDa molecular mass)
heme
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the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB)
heme
O88111; O88160
a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor
molybdenum cofactor
i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
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the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
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the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
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the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
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the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
[4Fe-4S]-center
O88111; O88160
a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor