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Investigation of the identity of an interstitial atom in the iron-molybdenum cofactor of nitrogenase.

机译:研究固氮酶的铁钼辅助因子中的间隙原子。

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摘要

The active site of the Molybdenum-dependent nitrogenase enzyme complex is a molybdenum and iron-containing cluster known as the FeMo-cofactor. This is represented as being a [7Fe-9S-Mo-X-homocitrate] cluster, where X denotes an unidentified small central atom. Previous studies have shown this to be carbon, nitrogen, or oxygen, and has been considered most likely to be nitrogen. To investigate the identity of X, spectroscopic analyses were performed on 15N-labeled or 13C-labeled MoFe protein and FeMo-cofactor which was isolated from the labeled protein. Spectroscopy was also performed on FeMo-cofactor as well as 15N-labeled FeMo-cofactor bound to nifX protein. These studies did not positively identify the central atom, but did provide some new information about the nature of FeMo-cofactor.
机译:钼依赖性固氮酶复合物的活性位点是被称为FeMo辅因子的钼和铁的簇。这表示为[7Fe-9S-Mo-X-单向]簇,其中X表示未识别的小中心原子。以前的研究表明,这是碳,氮或氧,被认为最有可能是氮。为了研究X的身份,对15N标记或13C标记的MoFe蛋白和从标记蛋白中分离出的FeMo辅因子进行了光谱分析。还对FeMo辅因子以及与nifX蛋白结合的15N标记的FeMo辅因子进行了光谱分析。这些研究没有积极地确定中心原子,但确实提供了有关FeMo辅因子性质的一些新信息。

著录项

  • 作者

    Maesar, Nathan Karl.;

  • 作者单位

    Utah State University.;

  • 授予单位 Utah State University.;
  • 学科 Chemistry Biochemistry.; Chemistry Inorganic.
  • 学位 M.S.
  • 年度 2007
  • 页码 88 p.
  • 总页数 88
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;无机化学;
  • 关键词

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