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CHEM203: Bioinorganic Chemistry

Unit 3: Metal Ion Transport and Storage   Transition-metal ions such as iron, copper, and zinc are essential components of key biological molecules that exist within all living organisms.  These metal ions are obtained by living organisms through their diet and then are transported into and stored by cells until they are needed for the synthesis of a particular protein or enzyme.  In this unit of the course, you will explore this process of transportation and storage in great detail.

Unit 3 Time Advisory
This unit should take you approximately 9.5 hours to complete.

☐    Subunit 3.1: 4 hours   

☐    Subunit 3.2: 1.5 hours

☐    Subunit 3.3: 0.5 hour

☐    Subunit 3.4: 0.5 hour

☐    Subunit 3.5: 2.5 hours

☐    Subunit 3.6: 0.5 hour

Unit3 Learning Outcomes
Upon successful completion of this unit, the student should be able to: - Identify the major types of metal-ion transport and storage macromolecules. - Discuss how common metal ions are absorbed, transported, and stored in biological systems. - Describe the importance of metal ions in protein and enzyme syntheses.

3.1 Transferrin   - Reading: Bioinorganic Chemistry: Dr. Elizabeth C. Theil and Dr. Kenneth N. Raymond’s “Chapter 1: Transition-Metal Storage, Transport, and Biomineralization” Link: Bioinorganic Chemistry: Dr. Elizabeth C. Theil and Dr. Kenneth N. Raymond’s “Chapter 1: Transition-Metal Storage, Transport, and Biomineralization” (PDF)
 
Instructions: Please click on the link above to access the webpage for the online textbook.  Then, click on the link for chapter 1 to open the PDF and read chapter 1 in its entirety.  You may also choose to download the PDF for the entire book by clicking on the link at the top of the webpage titled “PDF” and navigating to chapter 1 from there. As you progress through this reading, note the significance that a metal’s oxidation state, coordination chemistry, and abundance play in each of the systems described in the reading.  The unique properties of each metal determine the metal’s specificity for each system. 
 
Please note that this reading also covers material you need to know for subunits 3.2-3.4, found below.  When you reach those subunits, you may find it helpful to refer back to this reading for review.
 
This reading, including note-taking, should take you approximately 4 hours to complete.
  
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3.2 Ferritin   Note: Some of the material you need to know for this subunit is covered in the textbook reading assigned beneath subunit 3.1, found above.  You may find it helpful to refer back to that material as you complete the reading below.

  • Reading: Washington University in St. Louis: Dr. Rachel Casiday and Dr. Regina Frey’s “Iron Use and Storage in the Body: Ferritin and Molecular Representations” Link: Washington University in St. Louis: Dr. Rachel Casiday and Dr. Regina Frey’s “Iron Use and Storage in the Body: Ferritin and Molecular Representations” (HTML)

    Instructions: Please click on the link above to access and read the entire webpage tutorial on ferritin.  This tutorial features interactive models of ferritin – both alone and interacting with a peptide chain – that will help you gain a better understanding of the interactions among iron, ferritin, and larger biological systems. 

    This reading should take you approximately 1 hour and 30 minutes to complete. 
     
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3.3 Siderophores   Note: Some of the material you need to know for this subunit is covered in the textbook reading assigned beneath subunit 3.1, found above.  You may find it helpful to refer back to that material as you complete the reading below.

  • Reading: The Journal of Biological Chemistry 270, no. 45 (1995): Dr. J.B. Neilands’s “Siderophores: Structure and Function of Microbial Iron Transport Compounds” Link: The Journal of Biological Chemistry 270, no. 45 (1995): Dr. J.B. Neilands’s “Siderophores: Structure and Function of Microbial Iron Transport Compounds” (HTML)
     
    Instructions: Please click on the link above to access and read the entire journal article.  A PDF copy of this article also is available free-of-charge via the link titled “Full Text PDF” at the right of the webpage, should you wish to read the article in that format.  This reading provides you with a review of the structure and function of siderophores.  Siderophores are high-spin ligands with a specific affinity for the higher-oxidation-state Fe3+ ion.  This article also discusses the binding of siderophores in terms of hard/soft-acid/base (HSAB) theory.
     
    This reading should take you approximately 30 minutes to complete.
     
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3.4 Metallothioneins   Note: Some of the material you need to know for this subunit is covered in the textbook reading assigned beneath subunit 3.1, found above.  Section II.A.2 of the textbook, which begins on page 16, specifically covers metallothioneins; you may find it helpful to refer back to that section as you complete the reading below.

  • Reading: World Journal of Surgical Oncology 9, no. 54 (2011): N. Thirumoorthy et al.’s “A Review of Metallothionein Isoforms and their Role in Pathophysiology” Link: World Journal of Surgical Oncology 9, no. 54 (2011): N. Thirumoorthy et al.’s “A Review of Metallothionein Isoforms and their Role in Pathophysiology” (HTML)
      
    Instructions: Please click on the link above to access and read the entire journal article.  A PDF copy of the article also is available free-of-charge via the link titled “View PDF” at the right of the webpage, should you wish to read the article in that format.  This reading provides you with a review of the structure and physiological importance of metallothionein.  Specifically, the article examines the role of metallothioneins in cancer, bone-growth retardation, oxidative stress, kidney function, the central nervous system, heart disease, and diabetes. 
     
    This reading should take you approximately 30 minutes to complete.
      
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3.5 Copper-Transporting ATPases   - Reading: Physiological Reviews 87, no. 3 (2007): Svetlana Lutsenko et al.’s “Function and Regulation of Human Copper-Transporting ATPases” Link: Physiological Reviews 87, no. 3 (2007): Svetlana Lutsenko et al.’s “Function and Regulation of Human Copper-Transporting ATPases” (HTML)
     
Instructions: Please click on the link above to access and read the entire article.  A PDF copy of the article also is available free-of-charge via the link titled “Full Text (PDF)” at the right of the webpage, should you wish to read the article in that format.  This article provides information on the structure, mechanism, and regulation of Cu-ATPases.  As you read, pay particular attention to the structural motifs (the NH2 terminus, the ATP binding domain, and the COOH terminus) and their roles in binding and transport.
 
This reading should take you approximately 2 hours and 30 minutes to complete.
     
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3.6 Metallochaperones   - Reading: The Journal of Biological Chemistry 275, no. 33 (2000): Thomas V. O’Halloran and Valeria Cizewski Culotta’s “Metallochaperones, an Intracellular Shuttle Service for Metal Ions” Link: The Journal of Biological Chemistry 275, no. 33 (2000): Thomas V. O’Halloran and Valeria Cizewski Culotta’s “Metallochaperones, an Intracellular Shuttle Service for Metal Ions” (HTML)
 
Instructions: Please click on the link above to access and read the entire article.  A PDF copy of the article also is available free-of-charge via the link titled “Full Text (PDF)” at the right of the webpage, should you wish to read the article in that format.  This reading provides you with a review of the importance of metallochaperones in metal transport.  Copper is highly redox-active and would adversely affect cells if not transported to its proper activation site.  Metallochaperones provide safe transport of such metal ions to their intended destinations throughout the human body.
 
This reading should take you approximately 30 minutes to complete.
 
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