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Direct Measurement of the Nanomechanical Stability of a Redox Protein Active Site and Its Dependence upon Metal Binding
dc.contributor.author | Giannotti, Marina |
dc.contributor.author | Cabeza de Vaca, Israel |
dc.contributor.author | Artés, Juan M. |
dc.contributor.author | Sanz, Fausto |
dc.contributor.author | Guallar, Víctor |
dc.contributor.author | Gorostiza, Pau |
dc.contributor.other | Barcelona Supercomputing Center |
dc.date.accessioned | 2016-03-10T16:15:17Z |
dc.date.available | 2016-09-12T00:30:37Z |
dc.date.issued | 2015-09-10 |
dc.identifier.citation | Giannotti, Marina [et al.]. Direct Measurement of the Nanomechanical Stability of a Redox Protein Active Site and Its Dependence upon Metal Binding. "Journal of Physical Chemistry B", 10 Setembre 2015, vol. 119, núm. 36, p. 12050-12058. |
dc.identifier.issn | 1520-6106 |
dc.identifier.uri | http://hdl.handle.net/2117/84165 |
dc.description.abstract | The structural basis of the low reorganization energy of cupredoxins has long been debated. These proteins reconcile a conformationally heterogeneous and exposed metal-chelating site with the highly rigid copper center required for efficient electron transfer. Here we combine single-molecule mechanical unfolding experiments with statistical analysis and computer simulations to show that the metal-binding region of apo-azurin is mechanically flexible and that high mechanical stability is imparted by copper binding. The unfolding pathway of the metal site depends on the pulling residue and suggests that partial unfolding of the metal binding site could be facilitated by the physical interaction with certain regions of the redox protein. |
dc.description.sponsorship | We are grateful to A. Donaire and I. Díez-Pérez for discussions, and to the Catalan government (grant 2014SGR-1251), the Spanish government (grant CTQ2013-43892R) and the European Research Council (PELE ERC-2009-Adg 25027) for financial support. |
dc.format.extent | 8 p. |
dc.language.iso | eng |
dc.publisher | ACS Publications |
dc.subject | Àrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambiental |
dc.subject.lcsh | Protein |
dc.subject.other | Azurin |
dc.subject.other | Cupredoxins |
dc.subject.other | Force spectroscopy |
dc.subject.other | Nanomechanical stability |
dc.subject.other | Single molecule |
dc.title | Direct Measurement of the Nanomechanical Stability of a Redox Protein Active Site and Its Dependence upon Metal Binding |
dc.type | Article |
dc.subject.lemac | Proteïnes |
dc.identifier.doi | 10.1021/acs.jpcb.5b06382 |
dc.description.peerreviewed | Peer Reviewed |
dc.relation.publisherversion | http://pubs.acs.org/doi/abs/10.1021/acs.jpcb.5b06382?journalCode=jpcbfk |
dc.rights.access | Open Access |
dc.description.version | Postprint (author's final draft) |
dc.relation.projectid | info:eu-repo/grantAgreement/EC/FP7/250277/EU/P.E.L.E (Protein Energy Landscape Exploration): a la carte drug design tools/PELE |
dc.relation.projectid | info:eu-repo/grantAgreement/MINECO//CTQ2013-43892-R/ES/APLICACIONES TERAPEUTICAS DE LA OPTOFARMACOLOGIA/ |
local.citation.publicationName | Journal of Physical Chemistry B |
local.citation.volume | 119 |
local.citation.number | 36 |
local.citation.startingPage | 12050 |
local.citation.endingPage | 12058 |
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