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4Fe-4S cluster
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core extrusion experiments indicate 6 [4Fe-4S] clusters per tetramer, and electron paramagnetic resonance spectroscopy detects at least one of these clusters, in the reduced form
Co2+
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the multifunctional enzyme complex contains Co2+
Fe-S center
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the multifunctional enzyme complex contains iron-sulfur centers
S2-
contains a [NiFe4S5] center called cluster C
Zn2+
-
the multifunctional enzyme complex contains Zn2+
[2Fe-2S]-center
the small subunit contains two [2Fe-2S] centers
copper
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dinuclear heterometal [CuSMo(=O)OH] cluster in the active site
copper
contains copper, essential for activity
copper
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synthesis and characterization of dinuclear Mo-Cu complexes relevant to the active site of MoCu-enzyme by X-ray diffraction studies and by reactivity
Cu2+
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the enzyme contains copper
Cu2+
the native enzyme contains copper in the active site
Fe2+
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the enzyme contains iron
Fe2+
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contains 9 Fe+ per monomer
Fe2+
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contains a NiFe center, called C-cluster
Fe2+
contains a [NiFe4S5] center called cluster C
Fe2+
-
contains one Ni-4Fe-5S cluster
Fe2+
Ni-, Fe-, and S-containing metal center called cluster C
Fe2+
CODHII contains iron, the active site of CODH contains a [NiFe4S4OHx] cluster known as C-cluster
Fe2+
-
contains iron in form of Ni4Fe-4S clusters
Fe2+
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tightly bound by the enzyme
Fe2+
-
contains a NiFe center, called C-cluster
Fe2+
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contains a NiFe center, called C-cluster
Iron
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the alphabeta dimer contains approximately 9-11 mol of iron and 12-14 mol of acid-labile sulfur per mol of dimer
Iron
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61.5 mol nonheme iron per mol of complex
Iron
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[Ni-4Fe-4S] cluster or [Ni-4Fe-5S] cluster
Iron
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0.58, 0.67 and 1.96 atoms of iron per mol of large, medium- and small subunit, two iron-sulfur centers are associated with the small subunit
Iron
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contains 15.6 mol of iron per mol of alpha2beta oligomer
Iron
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contains 25 mol of Fe2+ and 20 mol of S2- per mol of tetramer, the enzyme contains 2 (4Fe-4S)+ clusters
Iron
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enzyme contains 3 iron containing centers: center A contains nickel and iron and is suggested to be the acetyl-CoA cleavage site, center B is a [4Fe-4S]2+/1+ center, center C is a fast relaxing center
Iron
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CO dehydrogenase complex consists of a two-subunit nickel/iron-sulfur component and the two-subunit factor III-containing corrinoid/iron-sulfur (Co/Fe-S) component
Iron
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the NiFe complex is required for catalyzing the exchange reaction and the acetyl-CoA synthase reaction
Iron
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CO oxidation occurs at Ni- and FeS containing center C, electrons are transferred from cluster C via center B to external electron acceptors
Iron
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the alphabeta dimer contains approximately 9-11 mol of iron and 12-14 mol of acid-labile sulfur per mol of dimer
Iron
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contains 11 mol of iron and 14 mol of acid-labile sulfur per mol of alphabeta dimer
Iron
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enzyme utilizes three types of Fe-S clusters: a [Ni4Fe5S] C-cluster catalyzing the CO oxidation, and 2 distinct [4Fe4S] electron-transfer sites called clusters B and D
Iron
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the enzyme contains two metal centers: a Ni-X-[4Fe-4S]2+/1+ cluster, i.e. C-center, that serves as the CO-oxidation site and a standard [Fe4S4]2+/1+ cluster, i.e. B-center, that mediates electron flow from the C-center to the external electron acceptor
Iron
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enzyme form I contains 7 iron and 6 sulfur per monomer
Iron
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enzyme form II contains 9 iron and 8 sulfur per monomer
Iron
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wild-type, 8.97 mol per mol of enzyme
Molybdenum
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molybdopterin-cytosine dinucleotide cofactor is composed of a molybdenum ion with 2 oxo- and 1 hydroxoligand complexed by the enedithiolene group of molybdopterin
Molybdenum
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dinuclear heterometal [CuSMo(=O)OH] cluster in the active site
Molybdenum
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the enzyme contains molybdenum
Molybdenum
contains molybdenum, essential for activity
Molybdenum
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2.29 mol/mol enzyme
Molybdenum
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synthesis and characterization of dinuclear Mo-Cu complexes relevant to the active site of MoCu-enzyme by X-ray diffraction studies and by reactivity
Ni2+
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contains 0.1 Ni2+ per monomer
Ni2+
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contains a NiFe center, called C-cluster
Ni2+
contains a [NiFe4S5] center called cluster C
Ni2+
-
contains one Ni-4Fe-5S cluster
Ni2+
Ni-, Fe-, and S-containing metal center called cluster C
Ni2+
CODHII contains nickel, the active site of CODH contains a [NiFe4S4OHx] cluster known as C-cluster
Ni2+
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required. Nickel is inserted into CODH without the need to express the native Ni insertase protein
Ni2+
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contains nickel in form of Ni4Fe-4S clusters
Ni2+
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tightly bound by the enzyme
Ni2+
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Ni is tightly bound to the enzyme and is not removed by anaerobic dialysis or gel permeation
Ni2+
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the multifunctional enzyme complex contains Ni2+
Ni2+
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contains a NiFe center, called C-cluster
Ni2+
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contains Ni2+-activated alpha subunits, Ni2+ is required for activity and oligomerization
Ni2+
-
contains a NiFe center, called C-cluster
Nickel
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the alphabeta dimer contains approximately 2 mol of nickel per mol of dimer
Nickel
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carbon monoxide dehydrogenase II, enzyme contains 5 metal clusters, a [Ni-4Fe-5S] cluster appears to be the active site of CO oxidation
Nickel
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3 mol per mol of complex
Nickel
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[Ni-4Fe-4S] cluster or [Ni-4Fe-5S] cluster
Nickel
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contains nickel in a NiFe3S4 cluster
Nickel
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contains 2 g-atoms of nickel per mol of enzyme
Nickel
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contains 1.3 mol of nickel per mol of alpha2beta2 oligomer
Nickel
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contains 1.3 mol of Ni2+ per mol of tetramer
Nickel
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CO dehydrogenase complex consists of a two-subunit nickel/iron-sulfur component and the two-subunit factor III-containing corrinoid/iron-sulfur (Co/Fe-S) component
Nickel
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the NiFe complex is required for catalyzing the exchange reaction and the acetyl-CoA synthase reaction
Nickel
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both CO and CoASH bind near the nickel site, nickel may therefore be the active metal center for C-C bond formation
Nickel
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contains 2 mol of nickel per mol of alphabeta dimer
Nickel
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contains 2-3 mol of nickel per mol of enzyme
Nickel
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the alphabeta dimer contains approximately 2 mol of nickel per mol of dimer
Nickel
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the enzyme contains two metal centers: a Ni-X-[4Fe-4S]2+/1+ cluster, i.e. C-center, that serves as the CO-oxidation site and a standard [4Fe-4S]2+/1+ cluster, i.e. B-center, that mediates electron flow from the C-center to the external electron acceptor, the nickel cation is proposed to be Ni2+ of the oxidized state of the C-center and in the one-electron-reduced state of the C-center, appears to strongly affect the redox behavior of the [4Fe-4S]2+/1+ component of the C-center
Nickel
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enzyme form I contains 0.6 mol of nickel per mol of monomer
Nickel
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enzyme form II contains 1.4 mol of nickel per mol of monomer
Nickel
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Ni-depleted enzyme is still able to produce formate
Nickel
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wild-type, 0.85 mol per mol of enzyme. Analysis of activation of wild-type and mutant apo-enzymes by nickel
Nickel
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synthesis of an analogue of the C-cluster of Carboxydothermus hydrogenoformans with a planar Ni(II) site and attachment of an exo iron atom in the core unit NiFe4S5 and analysis of products
Zinc
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the alphabeta dimer contains approximately 1 mol of zinc per mol of dimer
Zinc
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the alphabeta dimer contains approximately 1 mol of zinc per mol of dimer
Zinc
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contains 1 mol of zinc per mol of alphabeta dimer
Zinc
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enzyme form I contains 0.4 mol of zinc per mol of monomer
Zinc
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enzyme form II contains 0.8 mol of zinc per mol of monomer
additional information
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no stimulation by MgSO4, CoCl2, NiCl2 and ZnSO4
additional information
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the enzyme contains 30 Fe, 2 Ni, 1 Zn, and 1 Cu (per alpha 2 beta 2 enzyme)
additional information
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no oligomerization or activity in the presence of Co2+, Zn2+, and Cu2+, oligomerization but no exhibition of catalytic activity in the presence of Pd2+ and Pt2+