4.5 Article

Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)

期刊

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 21, 期 10, 页码 2873-2876

出版社

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2011.03.087

关键词

Aminopyrrolnitrin oxygenase (PrnD); Active site modeling; Electron transfer; Isc operon; Overexpression

资金

  1. Ministry of Education, Science and Technology [331-2007-1-D00144]
  2. NRF [2009-0077718]
  3. US Office of Naval Research [N00014-02-1-0725]
  4. National Research Foundation of Korea [2009-0077718] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

向作者/读者索取更多资源

Active site modeling of dimerization interface in combination with site-directed mutagenesis indicates that the electron in the PrnD Rieske oxygenase can be transferred by either of two pathways, one involving Asp183' and the other involving Asn180'. In addition, the overexpression of the isc operon involved in the assembly of iron-sulfur clusters increased the catalytic activity of PrnD in Escherichia coli by a factor of at least 4. (C) 2011 Elsevier Ltd. All rights reserved.

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