ENZYMOLOGY: Nickel to the Fore

作者: R. K. Thauer

DOI: 10.1126/SCIENCE.1064049

关键词: Active siteCrystal structureCrystallographyCarbon monoxideChemistryMetallurgyNickelMultidisciplinary

摘要: Nickel was long thought not to be important in biology, but now several enzymes are known depend on nickel for activity. In his Perspective, [Thauer][1] highlights the report by [ Dobbek et al .][2], whose high-resolution crystal structure of a enzyme reveals novel cluster active site. The offers surprising insights into site and likely mechanism through which harvests electrons from carbon monoxide. [1]: http://www.sciencemag.org/cgi/content/full/293/5533/1264 [2]: http://www.sciencemag.org/cgi/content/short/293/5533/1281

参考文章(13)
Matthew A. Pearson, Il-Seon Park, Ruth A. Schaller, Linda O. Michel, P. Andrew Karplus, Robert P. Hausinger, Kinetic and structural characterization of urease active site variants. Biochemistry. ,vol. 39, pp. 8575- 8584 ,(2000) , 10.1021/BI000613O
Wolfgang Grabarse, Felix Mahlert, Evert C. Duin, Marcel Goubeaud, Seigo Shima, Rudolf K. Thauer, Victor Lamzin, Ulrich Ermler, On the Mechanism of Biological Methane Formation: Structural Evidence for Conformational Changes in Methyl-Coenzyme M Reductase Upon Substrate Binding Journal of Molecular Biology. ,vol. 309, pp. 315- 330 ,(2001) , 10.1006/JMBI.2001.4647
H.-K. Loke, G. N. Bennett, P. A. Lindahl, Active acetyl-CoA synthase from Clostridium thermoaceticum obtained by cloning and heterologous expression of acsAB in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 97, pp. 12530- 12535 ,(2000) , 10.1073/PNAS.220404397
E Garcin, X Vernede, EC Hatchikian, A Volbeda, M Frey, JC Fontecilla-Camps, The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure. ,vol. 7, pp. 557- 566 ,(1999) , 10.1016/S0969-2126(99)80072-0
Ernest L. Maynard, Christopher Sewell, Paul A. Lindahl, Kinetic mechanism of acetyl-CoA synthase: steady-state synthesis at variable Co/Co2 pressures. Journal of the American Chemical Society. ,vol. 123, pp. 4697- 4703 ,(2001) , 10.1021/JA004017T
Jongyun Heo, Christopher R. Staples, Paul W. Ludden, Redox-dependent CO2 reduction activity of CO dehydrogenase from Rhodospirillum rubrum. Biochemistry. ,vol. 40, pp. 7604- 7611 ,(2001) , 10.1021/BI002554K
Gabriele B. Diekert, Ernst G. Graf, Rudolf K. Thauer, Nickel requirement for carbon monoxide dehydrogenase formation in Clostridium pasteurianum Archives of Microbiology. ,vol. 122, pp. 117- 120 ,(1979) , 10.1007/BF00408054
Ortwin Meyer, Lothar Gremer, Reinhold Ferner, Marion Ferner, Holger Dobbek, Manuel Gnida, Wolfram Meyer-Klaucke, Robert Huber, The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase. Biological Chemistry. ,vol. 381, pp. 865- 876 ,(2000) , 10.1515/BC.2000.108
Holger Dobbek, Vitali Svetlitchnyi, Lothar Gremer, Robert Huber, Ortwin Meyer, Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster Science. ,vol. 293, pp. 1281- 1285 ,(2001) , 10.1126/SCIENCE.1061500
Burt Zerner, Recent advances in the chemistry of an old enzyme, urease Bioorganic Chemistry. ,vol. 19, pp. 116- 131 ,(1991) , 10.1016/0045-2068(91)90048-T