1.2.5.3: aerobic carbon monoxide dehydrogenase
This is an abbreviated version!
For detailed information about aerobic carbon monoxide dehydrogenase, go to the full flat file.
Reaction
Synonyms
aerobic Mo/Cu-containing CO dehydrogenase, Carbon monoxide dehydrogenase, CO dehydrogenase, CODH, CoxS, coxSML, CutL, CutM, CutS, EC 1.2.2.4, EC 1.2.3.10, Mo-CODH, Mo-Cu carbon monoxide dehydrogenase, Mo/Cu CODH, MoCu-CODH, molybdenum- and copper-containing carbon monoxide dehydrogenase, molybdenum- and copper-dependent CO dehydrogenase, molybdenum-containing carbon monoxide dehydrogenase, molybdenum-containing CO dehydrogenase, molybdenum-copper carbon monoxide dehydrogenase, molybdenum-copper CO dehydrogenase, molybdenum/copper-containing carbon monoxide dehydrogenase, molybdoenzyme carbon monoxide dehydrogenase
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Metals Ions
Metals Ions on EC 1.2.5.3 - aerobic carbon monoxide dehydrogenase
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copper
Cu
Fe-S cluster
proximal Fe-S cluster I and distal Fe-S cluster II
Fe2+
iron-sulfur center
two [2Fe-2S] clusters in the small subunit
Mo
Molybdenum
Se
selenium
[2Fe-2S] cluster
[CuSMoO2] cluster
additional information
Fe2+
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the small subunit CoxS harbors two [2Fe-2S] iron-sulfur clusters
Mo
the pentacoordinated Mo(VI) exhibits a distorted square pyramidal coordination geometry. Function of the Mo ion in the proper orientation of active-site residues S-selanyl-Cys385 and Glu757. Mo is an absolute requirement for the conversion of molybdopterin to MCD, a tricyclic tetra-hydropterin-pyran system reduced by two electrons when compared to the fully oxidized state, as well as for the insertion of the Mocofactor into CODH
Molybdenum
in air-oxidized CO dehydrogenase, the oxidation state of Mo is +VI
Molybdenum
Mo/Cu-containing enzyme active site. The overall configuration of the binuclear center is L-MoVIO2-microS-CuI-Cys388, with L representing a bidentate pyranopterin cofactor common to all molybdenum enzymes other than nitrogenase
an S-selanylcysteine-containing large subunit
selenium
necessity of S-selanylcysteine for the catalyzed reaction, the selenium atom of S-selanylcysteine at the active site is located in a distance of 3.7 A from the Mo ion. It is near the equatorial oxo and hydroxo group of the Mo ion
a type I and a type II [2Fe-2S] center. The iron-sulfur protein carries the two [2Fe-2S] clusters, which can be distinguished by electron paramagnetic resonance spectroscopy
[2Fe-2S] cluster
the type II 2Fe:2S center is identified in the N-terminal domain and the type I center in the C-terminal domain of the iron-sulfur protein
[2Fe-2S] cluster
two distinct [2Fe-2S] clusters, the small subunit CoxS contains motifs indicative of type I and II [2Fe-2S] cluster, structure and binding strutcures, overview
[2Fe-2S] cluster
two types of [2Fe-2S] clusters, [2Fe-2S] clusters of type I and type II, the two [2Fe-2S] clusters are located in the S subunit. These prosthetic groups form a pathway for the electrons to the FAD. The C-terminal domain (residues 77-161) carries the proximal [2Fe-2S] cluster. The cluster is buried in CO dehydrogenase about 11 A below the protein surface at the interface between the S and the L subunit and is adjacent to the MCD-molybdenum cofactor. The [2Fe-2S] cluster is located at the N terminus of two alpha-helices that participate in a four-helix bundle of twofold symmetry
[2Fe-2S] cluster
two [2Fe-2S] iron-sulfur clusters in the small subunit
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CO oxidation by CO dehydrogenase proceeds at a unique [Mo+VIO2-S-Cu+I-S-Cys] cluster which matures posttranslationally while integrated into the completely folded apoenzyme. The Mo ion of the cluster is coordinated by the ene-dithiolate of the molybdopterin cytosine dinucleotide cofactor (MCD). The cofactor biosynthesis starts with the MgATP-dependent, reductive sulfuration of [MoVIO3] to [MoVO2SH] which entails the AAA+-ATPase chaperone CoxD. Then MoV is reoxidized and Cu1+-ion is integrated. Copper is supplied by the soluble CoxF protein which forms a complex with the membrane-bound von Willebrand protein CoxE through RGD-integrin interactions and enables the reduction of CoxF-bound Cu2+, employing electrons from respiration. Copper appears as Cu2+-phytate, is mobilized through the phytase activity of CoxF and then transferred to the CoxF putative copperbinding site. The coxG gene does not participate in the maturation of the bimetallic cluster
[CuSMoO2] cluster
the Mo-ion in the oxidized cluster is in +VI oxidation state and upon incubation with CO or sodium dithionite is reduced to Mo(IV). The Cu ion permanently remains in the +1 oxidation state. The ligands around Mo form a distorted square pyramidal geometry. The large subunit forms a molybdoprotein
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metal contents are determined by inductively coupled plasma atomic emission spectrometry
additional information
the binuclear active site contains copper as well as molybdenum
additional information
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the binuclear active site contains copper as well as molybdenum
additional information
the removal of Cu and S from the active site changes the functional [CuSMoO2] centre into a non-functional [MoO3] centre. The insertion of a sulfur atom from sodium sulfide into the [MoO3] center yielding a [MoO2S] center. The latter does not catalyze the oxidation of CO referring to a nonfunctional Mo-centre. Resulfuration of the [MoO3] centre and transfer of Cu from the Cu(I)thiourea complex to the [MoO2S] centre partially restores the specific CO oxidizing activity
additional information
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the enzyme contains 2.29 mol of Mo, 7.96 mol of Fe, 7.60 mol of S, and 1.99 mol of flavins at a 1.15:4:3.82:1 molar ratio, but contains no tungsten
additional information
the structure of the catalytically inactive Mominus CODH indicates that an intracellular Mo-deficiency affects exclusively the active site of the enzyme as an incomplete non-functional molybdenum cofactor is synthesized. The 5'-CDP residue is present in Mominus CODH, whereas the Mo-pyranopterin moiety is absent. In Moplus CODH the selenium faces the Mo ion and flips away from the Mo site in Mominus CODH