dc.creator | Cerqueira, Nuno M. F. S. A. | |
dc.creator | Fernandes, Pedro A. | |
dc.creator | González, Pablo Javier | |
dc.creator | Moura, José J. G. | |
dc.creator | Ramos, Maria J. | |
dc.date.accessioned | 2016-07-14T20:36:14Z | |
dc.date.accessioned | 2018-11-06T15:50:11Z | |
dc.date.available | 2016-07-14T20:36:14Z | |
dc.date.available | 2018-11-06T15:50:11Z | |
dc.date.created | 2016-07-14T20:36:14Z | |
dc.date.issued | 2013-09 | |
dc.identifier | Cerqueira, Nuno M. F. S. A.; Fernandes, Pedro A.; González, Pablo Javier; Moura, José J. G.; Ramos, Maria J.; The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase; American Chemical Society; Inorganic Chemistry; 52; 19; 9-2013; 10766-10772 | |
dc.identifier | 0020-1669 | |
dc.identifier | http://hdl.handle.net/11336/6501 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1901680 | |
dc.description.abstract | A structural rearrangement known as sulfur shift occurs in some Mo-containing enzymes of the DMSO reductase family. This mechanism is characterized by the displacement of a coordinating cysteine thiol (or SeCys in Fdh) from the first to the second shell of the Mo-coordination sphere metal. The hexa-coordinated Mo ion found in the as-isolated state cannot bind directly any exogenous ligand (substrate or inhibitors), while the penta-coordinated ion, attained upon sulfur shift, has a free binding site for direct coordination of the substrate. This rearrangement provides an efficient mechanism to keep a constant coordination number throughout an entire catalytic pathway. This mechanism is very similar to the carboxylate shift observed in Zn-dependent enzymes, and it has been recently detected by experimental means. In the present paper, we calculated the geometries and energies involved in the sulfur-shift mechanism using QM-methods (M06/(6-311++G(3df,2pd),SDD)//B3LYP/(6-31G(d),SDD)). The results indicated that the sulfur-shift mechanism provides an efficient way to enable the metal ion for substrate coordination. | |
dc.language | eng | |
dc.publisher | American Chemical Society | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ic3028034 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/ic3028034 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/10.1021/ic3028034 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | Molybdenum | |
dc.subject | Sulfur-shift | |
dc.subject | Nitrate reductase | |
dc.subject | Formate dehydrogenase | |
dc.title | The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |