Type:

Other

Description:

Access to the article is free, however registration and sign-in are required. Many organisms metabolize hydrogen gas by means of an enzyme called hydrogenase. The nature of the catalytic sites in the hydrogenases has long been a subject of conjecture and debate. In their Perspective, Adams and Stiefel discuss results reported in the same issue by Peters et al. in which x-ray crystallography was used to provide the first structural glimpse of the iron-only hydrogenase from the hydrogen-producing, anaerobic bacterium Clostridium pasteurianum. With this information, it is hoped that the properties of the hydrogenase enzyme can now be understood and possibly mimicked for chemical processing applications.

Subjects:

    Education Levels:

      Keywords:

      hydrogenase,protein structure,NSDL,NSDL_SetSpec_BEN,Life Science,oai:nsdl.org:2200/20110722030722706T,metabolism,fermentation

      Language:

      English

      Access Privileges:

      Public - Available to anyone

      License Deed:

      Creative Commons Attribution Non-Commercial Share Alike

      Collections:

      None
      This resource has not yet been aligned.
      Curriki Rating
      'NR' - This resource has not been rated
      NR
      'NR' - This resource has not been rated

      This resource has not yet been reviewed.

      Not Rated Yet.

      Non-profit Tax ID # 203478467