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New Insights Into the Transition of Iron-Sulfur Compounds From Minerals to Enzymes

Presenter: John Peters, Montana State University
When: November 28, 2011 11AM PST

Iron-sulfur proteins are ubiquitous and catalyze a number of reactions important to metabolic energy transformations and carbon and nitrogen fixation. The similarities between iron-sulfur motifs within proteins and minerals are too strong to be coincidental and as such relating the properties of iron-sulfur minerals and iron-sulfur clusters in proteins is a powerful approach for understanding the transition form the nonliving to the living Earth and the emergence of biology. Our most recent work has revealed that complex cofactors in biology are synthesized in complicated metabolic pathways that have evolved stepwise. Individual steps in the biosynthetic pathways strongly are analogous to mechanisms responsible for tuning prebiotic mineral reactivity including “ligand accelerated catalysis” and “organic nesting”. Insights into the origin and evolution of iron-sulfur enzymes and links to the RNA World will be presented.

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