Computational Study of the Fe(CN)(2)CO Cofactor and Its Binding to HypC Protein.

Albareda Contreras, Marta; Palacios Alberti, Jose Manuel; Imperial Ródenas, Juan y Fernandez Pacios, Luis (2013). Computational Study of the Fe(CN)(2)CO Cofactor and Its Binding to HypC Protein.. "Journal of Physical Chemistry B", v. 117 (n. 43); pp. 13523-13533. ISSN 1520-6106. https://doi.org/10.1021/jp407574n.

Descripción

Título: Computational Study of the Fe(CN)(2)CO Cofactor and Its Binding to HypC Protein.
Autor/es:
  • Albareda Contreras, Marta
  • Palacios Alberti, Jose Manuel
  • Imperial Ródenas, Juan
  • Fernandez Pacios, Luis
Tipo de Documento: Artículo
Título de Revista/Publicación: Journal of Physical Chemistry B
Fecha: 2013
Volumen: 117
Materias:
Escuela: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

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Resumen

In the intricate maturation process of [NiFe]-hydrogenases, the Fe(CN)2CO cofactor is first assembled in a HypCD complex with iron coordinated by cysteines from both proteins and CO is added after ligation of cyanides. The small accessory protein HypC is known to play a role in delivering the cofactor needed for assembling the hydrogenase active site. However, the chemical nature of the Fe(CN)2CO moiety and the stability of the cofactor–HypC complex are open questions. In this work, we address geometries, properties, and the nature of bonding of all chemical species involved in formation and binding of the cofactor by means of quantum calculations. We also study the influence of environmental effects and binding to cysteines on vibrational frequencies of stretching modes of CO and CN used to detect the presence of Fe(CN)2CO. Carbon monoxide is found to be much more sensitive to sulfur binding and the polarity of the medium than cyanides. The stability of the HypC–cofactor complex is analyzed by means of molecular dynamics simulation of cofactor-free and cofactor-bound forms of HypC. The results show that HypC is stable enough to carry the cofactor, but since its binding cysteine is located at the N-terminal unstructured tail, it presents large motions in solution, which suggests the need for a guiding interaction to achieve delivery of the cofactor.

Más información

ID de Registro: 26420
Identificador DC: http://oa.upm.es/26420/
Identificador OAI: oai:oa.upm.es:26420
Identificador DOI: 10.1021/jp407574n
URL Oficial: http://pubs.acs.org/doi/abs/10.1021/jp407574n
Depositado por: Memoria Investigacion
Depositado el: 26 Jun 2014 14:11
Ultima Modificación: 22 Sep 2014 11:41
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