Journal of Biological Chemistry
Volume 274, Issue 6, 5 February 1999, Pages 3331-3337
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ENZYMOLOGY
Carbon Monoxide and Cyanide as Intrinsic Ligands to Iron in the Active Site of [NiFe]-Hydrogenases: NiFe(CN)2CO, BIOLOGY'S WAY TO ACTIVATE H2*

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Infrared-spectroscopic studies on the [NiFe]-hydrogenase of Chromatium vinosum-enriched in15N or 13C, as well as chemical analyses, show that this enzyme contains three non-exchangeable, intrinsic, diatomic molecules as ligands to the active site, one carbon monoxide molecule and two cyanide groups. The results form an explanation for the three non-protein ligands to iron detected in the crystal structure of theDesulfovibrio gigas hydrogenase (Volbeda, A., Garcin, E., Piras, C., De Lacey, A. I., Fernandez, V. M., Hatchikian, E. C., Frey, M., and Fontecilla-Camps, J. C. (1996)J. Am. Chem. Soc. 118, 12989–12996) and for the low spin character of the lone ferrous iron ion observed with Mössbauer spectroscopy (Surerus, K. K., Chen, M., Van der Zwaan, W., Rusnak, F. M., Kolk, M., Duin, E. C., Albracht, S. P. J., and Münck, E. (1994) Biochemistry33, 4980–4993). The results do not support the notion, based upon studies of Desulfovibrio vulgaris [NiFe]-hydrogenase (Higuchi, Y., Yagi, T., and Noritake, Y. (1997) Structure5, 1671–1680), that SO is a ligand to the active site. The occurrence of both cyanide and carbon monoxide as intrinsic constituents of a prosthetic group is unprecedented in biology.

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This work was supported by the Netherlands Foundation for Chemical Research (SON) and the Netherlands Organization for Scientific Research (NWO).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

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Present address: TNO Nutrition and Food Research Institute, P. O. Box 360, NL-3700 AJ Zeist, The Netherlands.

Supported by a Cotrell College Science Award of Research Corp.