http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
An exemplary book providing a central source of information that summarizes the key features of the diverse and essential group of 2-oxoglutarate-dependent dioxygenases and related enzymes.
Cover; Preface; Contents; Chapter 1 Biochemical Diversity of 2-Oxoglutarate-Dependent Oxygenases; 1.1 Introduction; 1.2 2OG-Dependent Dioxygenases that Act on Proteins; 1.2.1 Protein Substrates with Structural Roles; 1.2.2 Protein Substrates with Oxygen-Sensing Roles; 1.2.3 Ribosomal Protein Hydroxylases; 1.2.4 Other Protein Substrates; 1.2.5 Histone Demethylases; 1.2.6 Other Protein Demethylases; 1.3 2OG-Dependent Dioxygenases that Act on DNA or RNA; 1.3.1 Demethylation of Alkylated DNA or RNA Substrates; 1.3.2 Other Oxidative Modifications of DNA or RNA.
1.4 Lipid-Related Metabolism Involving 2OG-Dependent Oxygenases1.5 Plant Metabolite Biosynthesis Using 2OG-Dependent Oxygenases; 1.5.1 2OG-Dependent Oxygenases in Flavonoid Biosynthesis; 1.5.2 2OG-Dependent Oxygenases of Gibberellin Biosynthesis; 1.5.3 2OG-Dependent Oxygenases in Alkaloid Synthesis; 1.5.4 Other Plant-Specific 2OG-Dependent Oxygenases; 1.6 2OG-Dependent Oxygenases Catalysing Reactions with Free Amino Acids, Nucleobases, Herbicides and Sulfur- or Phosphorous-Containing Compounds; 1.6.1 Amino Acid Hydroxylases; 1.6.2 Hydroxylases of Nucleobases and Nucleosides.
Chapter 3 Mechanisms of 2-Oxoglutarate-Dependent Oxygenases: The Hydroxylation Paradigm and Beyond3.1 Introduction; 3.2 Mechanism of the Fe/2OG Hydroxylases; 3.2.1 Evidence for Two Intermediates by Stopped-Flow Absorption Spectroscopy; 3.2.2 Evidence that the First Intermediate is a High-Spin Fe(iv) Complex; 3.2.3 Evidence that the Fe(iv) Complex Cleaves the C-H Bond of the Substrate; 3.2.4 Evidence that the Fe(iv) Complex is a Ferryl [Fe(iv)-Oxo] Species; 3.2.5 Evidence that the Second Intermediate is an Fe(ii) Product Complex.
[editors] Robert Hausinger, Christopher Schofield.