Metallocofactors that Activate Small Molecules

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.