Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.5.3 extracted from

  • Dobbek, H.; Gremer, L.; Meyer, O.; Huber, R.
    Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine (1999), Proc. Natl. Acad. Sci. USA, 96, 8884-8889.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.5.3

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion method using 0.8 M KH2PO4, 0.8 M NaH2PO4, 2% MPD, and 100 mM HEPES, pH 7.3, crystals containing cyanide are cocrystallized in the presence of 4 mM potassium cyanide, X-ray diffraction structure determination and analysis at 2.36-2.5 A resolution Afipia carboxidovorans

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Afipia carboxidovorans
Molybdenum in air-oxidized CO dehydrogenase, the oxidation state of Mo is +VI Afipia carboxidovorans
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 Afipia carboxidovorans
[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 Afipia carboxidovorans

Organism

Organism UniProt Comment Textmining
Afipia carboxidovorans P19919 and P19920 and P19921 genes coxL, coxM, and coxS
-

Reaction

Reaction Comment Organism Reaction ID
CO + a quinone + H2O = CO2 + a quinol hypothetical reaction mechanism, overview Afipia carboxidovorans
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO + a quinone + H2O
-
 Afipia carboxidovorans CO2 + a quinol
-
 ?

Subunits

Subunits Comment Organism
heterohexamer CO dehydrogenase is composed of an 88.7-kDa molybdoprotein (subunit L), a 30.2-kDa flavoprotein (subunit M), and a 17.8-kDa iron-sulfur protein (subunit S). It is organized as a dimer of LMS heterotrimers Afipia carboxidovorans

Cofactor

Cofactor Comment Organism Structure
FAD one noncovalently bound FAD molecule per monomer, FAD-binding occurs on the M subunit and requires conformational changes of subunit M introduced through the binding of subunt M to subunits LS. In air-oxidized CO dehydrogenase, the flavin is fully oxidized Afipia carboxidovorans
molybdopterin cofactor the L subunit carries the molybdenum cofactor, which is a mononuclear complex of Mo and molybdopterin-cytosine dinucleotide (MCD). The latter occurs in a redox state that is reduced by two electrons compared with the fully oxidized state, a tricyclic tetrahydropterin-pyran system. The MCD-molybdenum cofactor is buried at the center of the L subunit and is ligated through a dense network of hydrogen bonds originating from both domains of subunit L. The geometry of the first coordination sphere around the Mo ion is a distorted square pyramid Afipia carboxidovorans
additional information the enzyme is a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. The redox components of one LMS-structured monomer are the MCD-molybdenum cofactor, composed of a molybdenum ion with two oxo- and one hydroxoligand, complexed by the enedithiolene group of MCD, [2Fe-2S] clusters of type I and type II, and a noncovalently bound FAD molecule Afipia carboxidovorans

General Information

General Information Comment Organism
evolution CO dehydrogenase is a member of the xanthine oxidase family Afipia carboxidovorans