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Evidence that the C sub 1 site of carbon monoxide dehydrogenase (CODH) labeled with (1- sup 14 C)pyruvate differs from the binding site for CO

Conference · · FASEB Journal (Federation of American Societies for Experimental Biology); (United States)
OSTI ID:5266276
;  [1]
  1. Case Western Reserve Univ., Cleveland, OH (United States)
In the early studies with C. thermoaceticum, pyruvate and CoA were found essential for the synthesis of (2-{sup 14}C)acetyl-CoA with {sup 14}CH{sub 3}-tetrahydrofolate ({sup 14}CH{sub 3}-THF). Later, the enzymes catalyzing the acetyl-CoA pathway were purified and acetyl-CoA could be synthesized with CH{sub 3}THF, CoASH, CO or CO{sub 2} and H{sub 2}. CODH catalyzes the final step of the synthesis from bound CH{sub 3}, CO and CoASH groups. Pezacka and Wood using pyruvate ferredoxin oxidoreductase (PFOR) and CODH have shown that a {sup 14}C{sub 1}-CODH complex is formed from (1-{sup 14}C)pyruvate. This {sup 14}C{sub 1}-CODH complex was stable and could be separated from the (1-{sup 14}C)pyruvate. However with {sup 14}CO, no stable complex was observed. It has been determined in the present study that the {sup 14}C{sub 1}-CODH complex formed from (1-{sup 14}C)pyruvate is utilized for acetyl-CoA synthesis when both pyruvate and PFOR are present along with CH{sub 3}THF, CO and CoASH. These results suggest that the interaction between CODH and PFOR may be essential for the mobilization of the carboxyl group from pyruvate bound on CODH. Further studies are in progress to determine the amino acid(s)/site in CODH involved with (1-{sup 14}C)pyruvate and the interaction between PFOR and CODH in carboxyl transfer.
OSTI ID:
5266276
Report Number(s):
CONF-9104107--
Conference Information:
Journal Name: FASEB Journal (Federation of American Societies for Experimental Biology); (United States) Journal Volume: 5:4
Country of Publication:
United States
Language:
English