Metallocofactors that Activate Small Molecules: With Focus on Bioinorganic Chemistry

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Markus W. Ribbe

Metallocofactors that Activate Small Molecules

With Focus on Bioinorganic Chemistry

Markus W. Ribbe

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English

Springer Nature Switzerland AG
25 September 2020

Inorganic chemistry; Catalysis; Proteins; Enzymology; Biotechnology

Series: Structure and Bonding

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.

Edited by: Markus W. Ribbe
Imprint: Springer Nature Switzerland AG
Country of Publication: Switzerland
Edition: 2019 ed.
Volume: 179
Dimensions: Height: 235mm, Width: 155mm,
Weight: 454g
ISBN: 9783030258993
ISBN 10: 3030258998
Series: Structure and Bonding
Pages: 169
Publication Date: 25 September 2020
Audience: Professional and scholarly , Undergraduate
Format: Paperback
Publisher's Status: Active

Chapter 1. Looking at Nitrogenase: Insights from Modern Structural Approaches.- Chapter 2. Current Understanding of the Biosynthesis of the Unique Nitrogenase Cofactor Core.- Chapter 3. Recent Advances in the Chemical Synthesis of Nitrogenase Model Clusters.- Chapter 4. The Catalytic Mechanisms of the Molybdenum and Tungsten Enzymes.- Chapter 5. The Role of the Pyranopterin Dithiolene Component of Moco in Molybdoenzyme Catalysis.- Chapter 6. Mechanism of Ni,Fe-Containing Carbon Monoxide Dehydrogenases.

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.