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 unseen fold in PrPC, the observation of which provides new insight into the mechanism of prion disease.

Alzheimer’s disease (AD) is a progressive neurodegenerative disease, characterized by memory loss, motor skill loss, and eventually death that currently affects at least 5.8 million Americans.¹ This number is projected to more than double in the next 30 years.¹ Much effort has gone into determining the exact cause of onset of AD as well as developing strategies to mitigate its symptoms, however, there are currently are no substantial methods of prevention, slowing, or cure.¹ For nearly 30 years, the prevailing hypothesis for AD c

[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 industrial applications.

The growing demand for sources of clean and sustainable fuel has been at the forefront of research since the turn of the 21st century. Development of hydrogen fuel cells utilizes hydrogen to meet these demands. Traditionally platinum, the most expensive component, is employed at the cathode of these cells to catalyze the oxygen reduction reaction (ORR). The drive for a cheaper alternative has led to the study of iron porphyrin complexes, inspired by cytochrome c oxidase (CcO), to catalyze ORR.