Clostridium thermoaceticum nickel

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. 

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. 

Kumar, M., Lu, W.-P., and Ragsdale, S. W., 1994, Binding of carbon disufide to the site of acetyl-CoA synthesis by the nickel-iron-sulfur protein, CO dehydrogenase, from Clostridium thermoaceticum, Biochem. 33 976999777. 

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. 

Ragsdale, S. W., Wood, H. G., and Antholine, W. E., 1985, Evidence that an iron-nickel-carbon complex is formed by reaction of CO with the CO dehydrogenase from Clostridium thermoaceticum, Proc. Nad. Acad. Sci. USA 82 681196814. 

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... 

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