Tags: CMS Seminar


Toward Efficient Catalysts for Energy Conversion: from Enzymatic Function to Functional Mimics

Enzymes represent an invaluable source of inspiration for improving catalytic processes. In this talk I will highlight how theory and computation, tightly integrated with experiment, help elucidate enzymatic functionalities germane to the activation of energy-relevant small molecules and how these concepts can help design selective, efficient and sustainable bio-inspired catalysts. Specifically, I will discuss how hydrogenase enzymes finely…


Iron-sulfur cluster proteins as biological switches

Iron-sulfur cluster proteins carry out multiple functions, including as regulators of gene transcription/translation in response to environmental stimuli.  In all known cases, the cluster acts as the sensory module, where the inherent reactivity/fragility of iron-sulfur clusters with small/redox active molecules is exploited to effect conformational changes that modulate binding to nucleic regulatory sequences.  This promotes an often…


Novel intersection of mitochondrial fatty acid synthesis and iron-sulfur biogenesis

The mitochondrial acyl-carrier protein (ACP) functions in the synthesis of fatty acids within the mitochondrial matrix. Fatty acids are elongated on the covalently bound 4’-phosphopantetheine cofactor on ACP. ACP has a second essential function within the mitochondria in the biogenesis of iron-sulfur clusters. Cells depleted of ACP are impaired in FeS cluster formation throughout the cell. ACP is a stable subunit of the cysteine desulfurase (…


Photochemical reduction of redox enzymes for light-driven chemical reactions

Photosynthesis powers living cells through the photogeneration of electron-hole pairs that drive energy-demanding chemical reactions. The principles that enable photosynthesis and biological energy conversion also provide a foundation for advancing the development of artificial, light-driven systems for catalytic production of chemical fuels. In order to effectively couple catalysts with light-harvesting requires understanding how molecular…


Nitrogenase M-Cluster Assembly: Tracing the ‘9th Sulfur’ of the Nitrogenase Cofactor via a Semi-Synthetic Approach

The M-cluster is the active site of nitrogenase that contains an 8Fe-core assembled via coupling and rearrangement of two [Fe4S4] clusters concomitant with the insertion of an interstitial carbon and a ‘9th sulfur’. Combining synthetic [Fe4S4] clusters with an assembly protein template, we show that sulfite gives rise to the ‘9th sulfur’ that is incorporated in the catalytically important belt region of the cofactor after the radical SAM-…


Flavin Hydroperoxide: New tricks from an old dog

Since its discovery, in the early 1930s, the chemistry of riboflavin has been studied in great detail. It is therefore surprising that several new flavin-mediated reactions have been discovered over the past few years. My lecture will focus on three reactions where riboflavin is used as a substrate in a biosynthetic pathway. These reactions are involved in riboflavin catabolism, Vitamin B12 biosynthesis and roseoflavin biosynthesis.  


Unraveling Heme Metabolism in Malaria Parasites

Malaria remains a devastating infectious disease, with symptoms caused by Plasmodium parasite invasion of erythrocytes. During blood-stage infection, parasites import and digest up to 80% of host cell hemoglobin. This massive catabolic process liberates vast amounts of heme, which parasites detoxify by sequestering it into crystalline hemozoin within an acidic digestive vacuole. Eukaryotic Plasmodium parasites also require heme as a metabolic…
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