Ferredoxin [electronic resource] : NAD<sup>+</sup> oxidoreductase of <i>Thermoanaerobacterium saccharolyticum</i> and its role in ethanol formation [Identification of a ferredoxin NAD<sup>+</sup> oxidoreductase of <i>Thermoanaerobacterium saccharolyticum</i> and its role in ethanol formation]

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Tác giả:

Ngôn ngữ: eng

Ký hiệu phân loại: 668.5 Perfumes and cosmetics

Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2016

Mô tả vật lý: Size: p. 7134-7141 : , digital, PDF file.

Bộ sưu tập: Metadata

ID: 263392

 Ferredoxin:NAD<
 sup>
 +<
 /sup>
  oxidoreductase (NADH-FNOR) catalyzes the transfer of electrons from reduced ferredoxin to NAD<
 sup>
 +<
 /sup>
 . This enzyme has been hypothesized to be the main enzyme responsible for ferredoxin oxidization in the NADH-based ethanol pathway in <
 i>
 Thermoanaerobacterium saccharolyticum<
 /i>

  however, the corresponding gene has not yet been identified. Here, we identified the Tsac_1705 protein as a candidate FNOR based on the homology of its functional domains. We then confirmed its activity <
 i>
 in vitro<
 /i>
  with a ferredoxin-based FNOR assay. To determine its role in metabolism, the <
 i>
 tsac_1705<
 /i>
  gene was deleted in different strains of T. saccharolyticum. In wild-type <
 i>
 T. saccharolyticum<
 /i>
 , deletion of <
 i>
 tsac_1705<
 /i>
  resulted in a 75% loss of NADH-FNOR activity, which indicated that Tsac_1705 is the main NADH-FNOR in <
 i>
 T. saccharolyticum<
 /i>
 . When both NADH- and NADPH-linked FNOR genes were deleted, the ethanol titer decreased and the ratio of ethanol to acetate approached unity, indicative of the absence of FNOR activity. As a result, we tested the effect of heterologous expression of Tsac_1705 in Clostridium thermocellum and found improvements in both the titer and the yield of ethanol.
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