Clostridium thermoaceticum carbon monoxide dehydrogenase

Cramer, S.R, Eidsness, M.K., Pan, W.H., Morton, T.A., Ragsdale, S.W., Dervartanian, D.V, Ljungdahl, L.G. and Scott, R.A. (1987) X-Ray absorption spectroscopic evidence for a unique nickel site in Clostridium thermoaceticum carbon-monoxide dehydrogenase. Inorg. Chem., 26, 2477-2479. 

Sequence Comparison Between the N-Terminal Part of the Fepr Genes from Desulfovibrio desulfuricans (Dd) and Desulfovibrio vulgaris (Dv), Carbon Monoxide Dehydrogenase from Methanothrix soehngenii (Ms), Methanosarcina frisia Gdl (Mf), Clostridium thermoaceticum (Ct), Rhodospirillum rubrum (Rr), and Anaerobic Ribonucleotide Reductase from Escherichia coli (Ec) ... 

Drake HL. S-1 Hu, HG Wood (1980) Purification of carbon monoxide dehydrogenase, a nickel enzyme from Clostridium thermoaceticum. J Biol Chem 255 7174-7180. 

Huang S, PA Lindahl, C Wang, GN Bennett, EB Rudolph, JB Hughes (2000) 2,4,6-trinitrotolnene reduction by carbon monoxide dehydrogenase from Clostridium thermoaceticum. Appl Environ Microbiol 66 1474-1478. 

Xia J, Hu Z, Popescu CV, et al. 1997. Mossbauer and EPR study of the Ni-activated a-subunit of carbon monoxide dehydrogenase from Clostridium thermoaceticum. J Am Chem Soc 119 8301-12. 

Barondeau, D. P., and Lindahl, P. A., 1997, Methylation of carbon monoxide dehydrogenase from Clostridium thermoaceticum and mechanism of acetyl coenzyme A synthesis, J. Am. Chem. Soc. 119(17) 3959n3970. 

Fan, C., Gorst, C. M., Ragsdale, S. W., and Hoffman, B. M., 1991, Characterization of the Ni6 FeoC complex formed by reaction of carbon monoxide with the carbon monoxide dehydrogenase from Clostridium thermoaceticum by Q-band ENDOR, Biochem. 30 43In 435. 

Ragsdale, S. W., Clark, J. E., Ljungdahl, L. G., Lundie, L. L., and Drake, H. L., 1983, Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum a nickel, iron-sulfur protein, J. Biol. Chem. 258 2364n2369. 

Seravalli, J., Kumar, M., Lu, W.-P., and Ragsdale, S. W., 1997, Mechanism of carbon monoxide oxidation by the carbon monoxide dehydrogenase/acetyl-CoA syndiase from Clostridium thermoaceticum Kinetic characterization of the intermediates, Biochem. 36 11241fi 11251. 

Cd, and others. For example, nickel EXAFS of carbon monoxide dehydrogenase (CODH) from Clostridium thermoaceticum strain DSM 521 were collected and the Fourier filtered data was best fit to sulfur at 0.216 nm. A reasonable fit to oxygen/nitrogen could only be obtained by setting the zIEq to 40 and the Debye-Waller term to 5xl0 nm. A reasonable Ni-S fit was also obtained by assuming two Ni-S bond lengths at 0.222 and 0.211 nm, respectively. Addition of a Ni-M (M=Fe, Ni, Zn) term at 0.325 nm, also improved the... 

The reduction of 2,4-diamino-6-nitrotoluene was therefore investigated with hydrogenase purified from Clostridium pasteurianum and with carbon monoxide dehydrogenase partially purified from Clostridium thermoaceticum (39). In contrast to methods described in earlier publications, a test system was applied by which the nitro-reducing activity could be directly measured the consumption of DANT was assayed spectrophotometrically at 325 nm. 

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