In this case study, information is presented to students in the form of a dialog between a physician and two parents who have just learned that their child has thalassemia (Cooley’s Anemia). The treatment for this disorder requires a lifetime commitment to whole blood transfusion and chelation therapy (both administered on a daily to weekly basis); the biggest obstacle to long term survival is patient non-compliance.
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.
This suite of activities can be used as a unit exploring the use of small molecule models and biophysical techniques to illuminate complicated biomolecules. The Parent LO: Modeling the FeB center in bacterial Nitric Oxide reductase is a short, data-filled and well-written article that is approachable with an undergraduate's level of understanding.
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.
The following paper will be given to the students to study at home along with the questions in the attached document. Students will be allowed to discuss their answers in small groups and refine their answers, before the corresct answer is revealed.
The students will not need to see the actual spectra that are in the SI to be able to address the given questions, the spectra can be projected to the class when the answers of the student groups are discussed
Origins of Enantioselectivity during Allylic Substitution Reactions Catalyzed by Metallacyclic Iridium Complexes.
This is a problem set based on the article "Energetic Cuprous Azide Complex: Synthesis, Crystal Structure and Effection on the Thermal Decomposition of HMX" in the Journal of Chemical Crystallography. It has been used in a Chemistry Capstone course for both Chemistry and Biochemistry majors during the first semester senior year. Biochemistry majors are not required to take Inorganic Chemistry and Chemistry majors may be currently taking Inorganic chemistry.
In this literature discussion, students read a paper about a cobalt metallopeptide that imitates the active site of the enzyme nitrile hydratase. Specifically, the model complex is oxidized by air to produce a coordination sphere with both cysteine thiolate and sulfinic acid ligands, much like the post-translationally oxidized cysteine ligands in the biological system.
This is a literature discussion based on the paper “Spectroscopic Elucidation of the Inhibitory Mechanism of Cys2
This activity is designed to give students a deeper understanding of what post-translational modification does in a metalloenzyme using nitrile hydratase (NHase) as a model system. The metallo-active site of NHase contains a cobalt(III) center that is bound to an unusual coodination sphere containing bis-amidate, cysteinate, sulfenate (RSO-), and sulfinate (RSO2-) ligands.