Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.provenance | CONICET | - |
| dc.creator | Ferreiro, Dardo N. | - |
| dc.creator | Boechi, Leonardo | - |
| dc.creator | Estrin, Dario Ariel | - |
| dc.creator | Marti, Marcelo Adrian | - |
| dc.date | 2016-11-03T21:41:39Z | - |
| dc.date | 2016-11-03T21:41:39Z | - |
| dc.date | 2012-11-13 | - |
| dc.date | 2016-10-25T19:28:32Z | - |
| dc.date.accessioned | 2019-04-29T15:38:11Z | - |
| dc.date.available | 2019-04-29T15:38:11Z | - |
| dc.date.issued | 2012-11-13 | - |
| dc.identifier | Ferreiro, Dardo N.; Boechi, Leonardo; Estrin, Dario Ariel; Marti, Marcelo Adrian; The key role of water in the dioxygenase function of Escherichia coli flavohemoglobin; Elsevier; Journal Of Inorganic Biochemistry; 119; 13-11-2012; 75-84 | - |
| dc.identifier | 0162-0134 | - |
| dc.identifier | http://hdl.handle.net/11336/7968 | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/298192 | - |
| dc.description | Flavohemoglobins (FHbs) are members of the globin superfamily, widely distributed among prokaryotes and eukaryotes that have been shown to carry out nitric oxide dioxygenase (NOD) activity. In prokaryotes, such as Escherichia coli, NOD activity is a defence mechanism against the NO release by the macrophages of the hosts´ immune system during infection. Because of that, FHbs have been studied thoroughly and several drugs have been developed in an effort to fight infectious processes. Nevertheless, the protein´s structural determinants involved in the NOD activity are still poorly understood. In this context, the aim of the present work is to unravel the molecular basis of FHbs structural dynamics-to-function relationship using state of the art computer simulation tools. In an effort to fulfill this goal, we studied three key processes that determine NOD activity, namely i) ligand migration into the active site ii) stabilization of the coordinated oxygen and iii) intra-protein electron transfer (ET). Our results allowed us to determine key factors related to all three processes like the presence of a long hydrophobic tunnel for ligand migration, the presence of a water mediated hydrogen bond to stabilize the coordinated oxygen and therefore achieve a high affinity, and the best possible ET paths between the FAD and the heme, where water molecules play an important role. Taken together the presented results close an important gap in our understanding of the wide and diverse globin structural-functional relationships. | - |
| dc.description | Fil: Ferreiro, Dardo N.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina | - |
| dc.description | Fil: Boechi, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina | - |
| dc.description | Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina | - |
| dc.description | Fil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Elsevier | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jinorgbio.2012.10.015 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0162013412003571 | - |
| dc.rights | info:eu-repo/semantics/restrictedAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.source.uri | http://hdl.handle.net/11336/7968 | - |
| dc.subject | FLAVOHEMOGLOBIN | - |
| dc.subject | MOLECULAR DYNAMICS | - |
| dc.subject | PROTEIN ELECTRON TRANSFER | - |
| dc.subject | OXYGEN STABILIZATION | - |
| dc.subject | Otras Ciencias Químicas | - |
| dc.subject | Ciencias Químicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | The key role of water in the dioxygenase function of Escherichia coli flavohemoglobin | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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