Tags: CMS Seminar


How Metal Ions in the Brain Tip the Toxic Balance of the Killer Prion Protein

A prion is a misfolded form of the cellular prion protein, PrPC. Although the role of PrP in neurodegeneration was established over 30 years ago, there is little understanding of the protein’s normal function, and how misfolding leads to profound disease. Recent work shows that PrPC coordinates the cofactors Cu2+ and Zn2+, and regulates the distribution of these essential metal ions in the brain. Moreover, these metals stabilize a previously…


Unexpected oxygen tolerance in an efficient hydrogen-producing [FeFe] hydrogenase from Clostridium beijerinckii

[FeFe] hydrogenases catalyze reversible hydrogen evolution at rates as high as 10,000 turnovers per second. This exceptional catalytic ability is very attractive for the use of hydrogenases in renewable energy applications and biohydrogen production. Unfortunately, enzymes of this class are known to degrade irreversibly upon exposure to small  amounts of oxygen, presenting major roadblocks for study and implementation in practical or…


Lactate Racemase and its Novel Nickel-Pincer Nucleotide Cofactor

Lactic acid, a central metabolic intermediate of many cells, occurs as L- and D-isomers that are interconverted by lactate racemase. This enzyme from Lactobacillus plantarum is encoded by LarA and harbors a tethered nickel-pincer nucleotide (NPN) coenzyme derived from niacin. Synthesis of the enzyme-bound cofactor requires LarB, a carboxylase/hydrolase of nicotinic acid adenine dinucleotide (NaAD); LarE, a Mg·ATP-dependent sacrificial sulfur…


Ancient enzymology. Formate dehydrogenases and the reduction of CO2

We have examined the rapid reaction kinetics and spectroscopic properties of the molybdenum-containing, NAD+-dependent FdsABG formate dehydrogenase from C. necator, demonstrating the direct transfer of the substrate Ca hydrogen to the molybdenum center of the enzyme in the course of the reaction. In light of recent advances in our understanding of the structure of the molybdenum center propose a reaction mechanism involving direct hydride…


"Metaling" with Nature: Design and characterization of model metalloenzymes for small molecule activation


The intersection of nutrition and infection at the host-pathogen interface

All cells require nutrient metal to carry out essential biochemical processes. This requirement is something that the vertebrate immune system has exploited as a strategy to defend against infection by restricting microbial access to nutrient metal. This process of nutrient restriction during infection is called “nutritional immunity”. Bacterial pathogens have evolved elaborate mechanisms to circumvent nutritional immunity and acquire metal…


Dark Matter of Energy Conservation: Evolving Novel Metalloprotein Supercomplexes to Perform Unexpected Life Chemistries

All living organisms conserve energy by catalyzing redox biochemical reactions, which constitute respiration.  In most cases, respiration is achieved through the action of metalloenzymes and electron-transfer networks, wherein oxidation of reduced substrates is coupled to reduction of cofactors that pass along the electrons to a terminal oxidant.  The latter is O2 in aerobic respiration and eukaryotes have no respiratory flexibility at…


Spectroscopic and Kinetic Studies of Catalytically Versatile Non-Heme Iron Enzymes

Iron(II) and 2-Oxoglutarate (2OG) dependent non-heme iron (Fe(II)/2OG) enzymes catalyze a large array of chemical transformations, including hydroxylation, desaturation, epoxidation, halogenation, epimerization, endoperoxidation, as well as ring expansion/contraction reactions. Many of these transformations are key chemical steps in the biosynthesis of natural products having antibiotic and antimicrobial activities. In recent years, studies on…


New roles for aerobic hydrogen metabolism: from enzymes to ecosystems

Diverse microorganisms consume and produce hydrogen gas (H2) using metalloenzymes called hydrogenases. While this metabolism is traditionally associated with anaerobes, several lineages of bacteria and archaea are known to support aerobic growth on H2. In this seminar, I will reveal that the dominant bacteria inhabiting global soil ecosystems are also facultative H2 oxidisers. These bacteria use atmospheric H2 as a respiratory electron donor to…


Signaling through Hydrogen Sulfide

Toxic at high levels, H2S modulates a range of physiological processes. Biogenesis of H2S synthesis piggybacks on enzymes that catalyze alternative canonical reactions but switch metabolic tracks to meet cellular needs. We will discuss how H2S oxidation and signaling are regulated in colon, which is routinely exposed to high H2S of microbial origin.  
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