A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Export

@article{citeulike:2967598, abstract = {A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.}, address = {Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.}, author = {Doukov, T. I. and Iverson, T. M. and Seravalli, J. and Ragsdale, S. W. and Drennan, C. L.}, citeulike-article-id = {2967598}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1075843}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/12386327}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=12386327}, day = {18}, doi = {10.1126/science.1075843}, issn = {1095-9203}, journal = {Science (New York, N.Y.)}, keywords = {carbon\_monoxide\_dehydrogenase}, month = {October}, number = {5593}, pages = {567--572}, posted-at = {2008-07-06 18:34:06}, priority = {2}, title = {A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase.}, url = {http://dx.doi.org/10.1126/science.1075843}, volume = {298}, year = {2002} }

TY - JOUR ID - citeulike:2967598 L3 - citeulike-article-id:2967598 N2 - A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit. IS - 5593 JF - Science (New York, N.Y.) SN - 1095-9203 AD - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. EP - 572 TI - A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. VL - 298 SP - 567 KW - carbon_monoxide_dehydrogenase AU - Doukov, TI AU - Iverson, TM AU - Seravalli, J AU - Ragsdale, SW AU - Drennan, CL PY - 2002/10/18/ UR - http://dx.doi.org/10.1126/science.1075843 ER -