CHEM 0230

Bioinorganic Chemistry

Bioinorganic Chemistry
Life depends on the proper functioning of proteins and nucleic acids that are often metalated. In this course we will study the structure and function of metalloproteins and other metallobiomolecules. We will begin with an overview of bioinorganic chemistry. Next, we will look at two classic questions in bioinorganic chemistry. (1) How does hemoglobin cooperatively bind dioxygen? and (2) Why is cis-platin an anti-cancer drug whereas trans-platin is not? We will then spend the rest of the first half of the course learning the inorganic chemistry that will allow us to answer these questions and many others: simple bonding, symmetry, transition metal chemistry, and ligand field theory. In the second half of the course, we will start with some biochemistry fundamentals and then move on to case studies of zinc, iron, copper proteins, and metals in medicine. The textbooks will be Inorganic Chemistry by Miessler, Fisher, and Tarr, and Biological Inorganic Chemistry by Crichton, both available on-line for free. (CHEM0104 or CHEM0107) 3hrs lect/disc
Chemistry and Biochemistry
Chemistry & Biochemistry
Natural Sciences
Requirements Fulfilled:

Sections in Spring 2019

Spring 2019

CHEM0230A-S19 Lecture (Larrabee)