David R. Benson

Undergraduate Research Program Poster

The chemistry and biochemistry of heme proteins.

Heme is an iron-containing macrocycle that is an integral component of many proteins in bacteria, plants and animals. It is the part of hemoglobin that gives blood its red color. Heme proteins participate in a wide array of biological processes, including transport and storage of dioxygen (hemoglobin and myoglobin, respectively), electron transport (b and c cytochromes), breakdown of hydrogen peroxide (peroxidases and catalases), and hydrocarbon oxidation (cytochrome P450).

Several recently discovered heme proteins function as sensors for small molecules such as CO and O2.Part of our group’s research effort is directed toward design and synthesis of molecules that contain structural features common to these heme proteins, but which are smaller and therefore easier to study. We have adopted a multidisciplinary chemical approach to investigate how changes introduced into these model compounds influence their structure and function, in order that we may better understand how nature has fine-tuned the corresponding natural proteins to carry out their roles with remarkably high efficiency and specificity.

Our studies of model heme proteins are complemented by investigations of their natural counterparts, projects which provide students with the opportunity to also learn some basic techniques of biochemistry and molecular biology.An example is cytochrome b5, an electron transfer protein found in animals and plants.