College of Letters & Science

Permanent URI for this communityhttps://scholarworks.montana.edu/handle/1/37

The College of Letters and Science, the largest center for learning, teaching and research at Montana State University, offers students an excellent liberal arts and sciences education in nearly 50 majors, 25 minors and over 25 graduate degrees within the four areas of the humanities, natural sciences, mathematics and social sciences.

Browse

Filters

20141

Settings

Author: search.filters.author.Peters, John W.Subject: search.filters.subject.Inorganic chemistry

Search Results

Now showing 1 - 1 of 1
  • Thumbnail Image
    Item
    Radical S -Adenosyl-l-methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors
    (2014-12) Byer, Amanda S.; Shepard, Eric M.; Peters, John W.; Broderick, Joan B.
    Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors with biologically unusual non-protein ligands. The FeMo cofactor of nitrogenase has a MoFe7S9 cluster with a central carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cyanide and CO ligands as well as dithiomethylamine; the [Fe]-hydrogenase cofactor has CO and guanylylpyridinol ligands at a mononuclear iron site. Intriguingly, radical S-adenosyl-L-methionine enzymes are vital for the assembly of all three of these diverse cofactors. This minireview presents and discusses the current state of knowledge of the radical S-adenosylmethionine enzymes required for synthesis of these remarkable metal cofactors.
Copyright (c) 2002-2022, LYRASIS. All rights reserved.