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Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments.
Sickerman, Nathaniel S; Tanifuji, Kazuki; Hu, Yilin; Ribbe, Markus W.
Afiliação
  • Sickerman NS; Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, 92697-3900, USA.
  • Tanifuji K; Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, 92697-3900, USA.
  • Hu Y; Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, 92697-3900, USA.
  • Ribbe MW; Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, 92697-3900, USA.
Chemistry ; 23(51): 12425-12432, 2017 Sep 12.
Article em En | MEDLINE | ID: mdl-28726330
ABSTRACT
Nitrogenase is the only known biological system capable of reducing N2 to NH3 , which is a critical component of bioavailable nitrogen fixation. Since the discovery of discrete iron-sulfur metalloclusters within the nitrogenase MoFe protein, synthetic inorganic chemists have sought to reproduce the structural features of these clusters in order to understand how they facilitate the binding, activation and hydrogenation of N2 . Through the decades following the initial identification of these clusters, significant progress has been made to synthetically replicate certain compositional and functional aspects of the biogenic clusters. Although much work remains to generate synthetic iron-sulfur clusters that can reduce N2 to NH3 , the insights borne from past and recent developments are discussed in this concept article.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Coenzimas / Molibdoferredoxina Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Coenzimas / Molibdoferredoxina Idioma: En Ano de publicação: 2017 Tipo de documento: Article