Carbon monoxide dehydrogenase CODH

There are now three different proteins of the XDH/XO family whose structures have been determined by X-ray protein crystallography. The structure of aldehyde oxidoreductase from the bacterium Desulfovibrio gigas was the first X-ray structure determined for an oxo-molybdenum enzyme (17) and has been followed by stmctures of XO/XDH (10) and carbon monoxide dehydrogenase (CODH) (19, 21). Although the three enzymes are placed in the same family, there are structural differences among them at the active site and at the phosphate remote from the Mo center. 

Carbon monoxide dehydrogenase/acetyl coenzyme A synthase (CODH/ACS) describes two different classes of enzymes carbon monoxide dehydrogenase (CODH) isolated from Rhodospirillum rubrum or Carboxydothermus hydrogenoformans reversibly oxidizes CO to CO2 according to equation (2), and the bifunctional CODH/ACS enzyme from Moorella thermoacetica catalyzes the reversible reduction of CO2 to CO (CODH) and acetyl coenzyme assembly/disassembly (ACS) (equation 3). ... 

Carbon-monoxide dehydrogenase (CODH) and acetyl-coenzyme A synthetase... 

Conceptually, the simplest way to synthesize an organic molecule is to construct it one carbon at a time (Ragsdale and Pierce, 2008). The Woods—Ljungdahl pathway (Figure 15.3) does just that, synthesising acetyl-CoA from CO2. Carbon monoxide dehydrogenase, CODH and acetyl-CoA synthase, ACS are responsible for the reduction of CO2 to CO and the subsequent formation of acetyl-CoA (Drennan et al., 2004). CODH/ACS... 

The bifunctional carbon monoxide dehydrogenase (CODH)/acetyl-CoA synthase enzyme is a key enzyme involved in the Wood-Ljungdahl pathway of carbon fixation that operates in anaerobic bacteria. As such, it is a major player in the global carbon cycle. The CODH component of the enzyme catalyzes the reversible reduction of CO2 to CO (Equation (15)), which is then channeled to the ACS active site where it reacts with CoA and a methyl group provided by the corrinoid iron-sulfur protein (CFeSP) to form acetyl-CoA 30 (Equation (16)). 

S-adenosylmethionine (SAM or AdoMet) superfamily, aconitase, and others), enzymes that contain Fe-S heteroatomic clusters (nitrogenase iron-molybdenum cofactor (FeMoco), carbon monoxide dehydrogenase (CODH), and acetyl CoA synthase (ACS)), and enzymes that contain unique ligation sets around specialized iron centers ([NiFe] and [FeFe] hydrogenases) (Figure 1). ... 

Several important homogeneous catalytic reactions (e.g. hydroformylations) have been accomplished in water by use of water-soluble catalysts in some instances water can act as a solvent and as a reactant for hydroformylation. In addition, formation of aluminoxanes by partial hydrolysis of alkylaluminum halides results in very high activity bimetallic Al/Ti or Al/Zr metallocene catalysts for ethene polymerization which would be otherwise inactive. Polymerization of aryl diiodides and acetylene gas has recently been achieved in water with palladium catalysts. Finally, nickel-containing enzymes, such as carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase, operate in water with reaction mechanisms comparable with those of the WGSR or of the Monsanto methanol-to-acetic-acid process. ... 

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