This lecture provides a short introduction to the other half of biological iron chemistry: enzymes that do not contain a porphyrin group that ligates the iron atom. There are several important applications for non-heme iron in cells, both mammalian and bacterial. Oxygen activating non-heme iron enzymes fall into a few basic categories and includes mononuclear iron monooxygenases and dioxygenases, and binuclear iron monooxygenases. The requirements to activate and utilize dioxygen will be given. Examples of each type of enzyme, along with interesting catalytic intermediates implicated in their mechanisms, and the general catalytic cycles will be given.
|Dioxygen Activation in Nonheme Iron Enzymes (PPTX)||665.4 KB|
|Dioxygen Activation in Nonheme Iron Enzymes (PDF)||553.11 KB|
- The student will be able to identify the basic roles of non-heme iron in biology.
- The student will develop an understanding of the utility of building an enzyme with non-heme iron instead of heme iron in oxygen activation chemistry.
- The student will be able to demonstrate the need for external reducing equivalents in dioxygen activation.
- An advanced student will be able to apply this knowledge to choose the most appropriate enzyme type for a given chemical reaction.
This 5 slides would fit well after heme iron enzymes have been introduced. To make the best use of the slides, students should be familiar with the iron-oxo motif in bioinorganic chemistry and what its reactivity is.
An interesting discussion to have with your class would be to come up with some ideas as to why nature would choose to utilize non-heme iron over heme iron for use in oxidases. Generally, heme iron enzymes are capable of oxidizing any C-H bond (with the possible exception of methane), so issue really becomes one of nature trying to avoid "bringing a gun to a knife fight" in terms of substrate oxidation.