© 2019

Metallocofactors that Activate Small Molecules

With Focus on Bioinorganic Chemistry

  • Markus W. Ribbe

Part of the Structure and Bonding book series (STRUCTURE, volume 179)

Table of contents

  1. Front Matter
    Pages i-vii
  2. Belinda B. Wenke, Thomas Spatzal
    Pages 1-13
  3. Caleb J. Hiller, Lee A. Rettberg, Chi Chung Lee, Martin T. Stiebritz, Yilin Hu
    Pages 15-31
  4. Andrew M. Crawford, Julien J. H. Cotelesage, Roger C. Prince, Graham N. George
    Pages 63-100
  5. Sharon J. Nieter Burgmayer, Martin L. Kirk
    Pages 101-151
  6. Back Matter
    Pages 167-169

About this book


This volume highlights recent progress on the fundamental chemistry and mechanistic understanding of metallocofactors, with an emphasis on the major development in these areas from the perspective of bioinorganic chemistry. 

Metallocofactors are essential for all forms of life and include a variety of metals, such as iron, molybdenum, vanadium, and nickel. Structurally fascinating metallocofactors featuring these metals are present in many bacteria and mediate remarkable metabolic redox chemistry with small molecule substrates, including N2, CO, H2, and CO2. Current interest in understanding how these metallocofactors function at the atomic level is enormous, especially in the context of sustainably feeding and fueling our planet; if we can understand how these cofactors work, then there is the possibility to design synthetic catalysts that function similarly. 


Nitrogenase Molybdopterin Molybdopterin Models Carbon Monoxide Dehydrogenase Nitrogenase Cofactors

Editors and affiliations

  • Markus W. Ribbe
    • 1
  1. 1.Departments of Molecular Biology & Biochemistry, and ChemistryUniversity of CaliforniaIrvineUSA

About the editors

The focus of Dr. Ribbe’s research is the assembly and mechanism of nitrogenase, one of the most complex metalloenzymes known to date. Nitrogenase can be appreciated from the perspective of the useful agricultural and industrial products it generates, namely, ammonia, hydrogen and hydrocarbons. Since the beginning of his independent career, Dr. Ribbe has focused his efforts on investigating the biosynthesis of the Mo-nitrogenase from Azotobacter vinelandii and, in particular, the unique metal centers of its MoFe protein component: FeMoco and P-cluster. Results of these studies have firmly established nitrogenase MoFe protein as a model system that could be used to deduce the general mechanism of metal cluster assembly and develop successful strategies for synthesizing bio-inspired catalysts for industrial usage. Recently, Dr. Ribbe expanded his research to the investigation of the structure and function of the “alternative” V-nitrogenase from Azotobacter vinelandii. His discovery that V-nitrogenase can convert CO to hydrocarbons provides a potential blueprint for developing cost-efficient processes for industrial production of biofuels in the future.

Bibliographic information