A hyperthermophilic Ni-Fe hydrogenase drives the reduction of pyruvate to lactate in a cell-free system

The group of Yunhong SONG at CAS Institute of Industrial Biotechnology in Tianjin cloned a soluble enzyme I (SHI) from Pyrococcus furiosus and overexpressed it in Thermococcus kodakarensis. Purification was achieved in one step using a nickel-loaded column. The rSHI purified by this method was coupled with an FMN-containing diaphorase (DI) to form a new electron transport chain. which utilized hydrogen as a reducing agent to regenerate NADH, used to convert pyruvic acid into lactic acid.

CAS news release, November 5, 2018

Most popular posts:

This website stores cookies on your computer. These cookies are used to provide a more personalized experience and to track your whereabouts around our website in compliance with the European General Data Protection Regulation. If you decide to to opt-out of any future tracking, a cookie will be setup in your browser to remember this choice for one year.

Accept or Deny