I am a bioinorganic chemist. Because we work largely with enzymes containing
metal atoms in the active sites, we are also known as metalloenzymologists.
An enzyme is a biological catalyst, a protein that speeds up one particular
reaction. The enzyme I study, called carbon monoxide
dehydrogenase/acetyl-coenzyme A synthase (CODH/ACS) from the bacterium
Moorella thermoacetica, is unusual for several reasons:
- Is is bifunctional, which means one enzyme
catalyzes two different reactions
- Both reaction centers are connected by a molecular
- It supports a Ni-CH3 bond, one of
only two organometallic bonds known in an enzyme.
- It contains a nickel, iron, and sulfur atoms in both
active sites. Only four other types of enzymes have nickel in them
- The combination of Ni, Fe, and S in one place is
eerily similar to the catalyst needed to do what is thought to be the first
reaction that lead to the formation of life on Earth: the formaiton of
the C-C bond from methane and carbon dioxide.
I describe here the research I did on this enzyme.
- Postal address
Department of Chemistry, M.S. 179, Utah Valley State College, 800 W. University Parkway, Orem, Utah, 84058
- Electronic mail