2011 Annual Science Report
Montana State University Reporting | SEP 2010 – AUG 2011
Radical SAM Chemistry and Biological Ligand Accelerated Catalysis
A number of key reactions in biological systems are catalyzed by iron-sulfur enzymes. Iron-sulfur clusters in biology have a number of features in common with iron-sulfur minerals and their derivatives. We are using iron sulfur motifs as a model system to understand how chemistry in the abiotic mineral world was incorporated into biology on a path to the origin of life. We have found that iron-sulfur motifs in biology are synthesized and modified by reactions and mechanisms that we envision minerals could have been modified on the early prebiotic Earth. The results have had a profound impact on our ability to understand a stepwise trajectory from the nonliving to the living Earth.
Iron-sulfur clusters are thought to be among the most ancient cofactors in living systems. The Fe-S enzyme thrust is focused on examining the structure, mechanism, and biosynthesis of the complex Fe-S enzymes nitrogenase and hydrogenase. Exciting new results have identified important links between the biosynthesis of the H-cluster and FeMo-co and have provided direct links to the evolution of Fe-S biocatalysts from their mineral-based precursors.
PROJECT INVESTIGATORS:Joan Broderick
PROJECT MEMBERS:John Peters
RELATED OBJECTIVES:Objective 3.1
Sources of prebiotic materials and catalysts
Origins and evolution of functional biomolecules
Origins of energy transduction