This "Five slides about" is meant to introduce faculty and/or students to Spectroelectrochemistry (SEC), a technique that is used in inorganic chemistry research and other areas. SEC is a powerful tool to examine species that are normally hard to synthesize and isolate due to instability and high reactivity. Papers with examples of SEC techniques are provided on the last slide. 

These slides describe the recent literature on the structure of the iron sulfur cluster of nitrogenase active site, FeMo-co.  Included are: a comparison of industrial vs. biological ammonia production, several crystal structures from the literature including the unknown until recently hypervalent carbon atom in the center, and a brief mention of the troubling sterics of the active site as crystallized.

These Five Slides About examine the structure and function of the iron binding and transport protein transferrin. Students learn that transferrin also acts as an iron buffer and as a potential antimicrobial agent. The structure of the protein is explored in detail; it consists of a single polypeptide (80kDa) folded into two lobes, each of which can bind a single iron in a high affinity region. Changes in the protein as a result of iron uptake is discussed. The iron binding region and the requirement of a bidentate synergistic anion (carbonate) are examined.

Over several decades of teaching General Chemistry I have utilized various methods to get students to draw appropriate Lewis Dot Structures. About 10 years ago I learned about a process which I call the "Account Ledger Method". In this method all valence electrons are assumed to initially belong to the molecule (and placed in a ledger) and not to specific individual atoms. As the molecule is put together those electrons are distributed systematically and removed from the ledger.