References

1. Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC. (2001). The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Retrieved from http://www.nature.com/nsmb/journal/v8/n2/full/nsb0201_156.html

2. Amy Medlock, Larkin Swartz, Tamara A. Dailey, Harry A. Dailey, and William N. Lanzilotta. (2007). Substrate interactions with human ferrochelatase. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1794275/?tool=pmcentrez

3. MichaelW. King. (2010). Erythropoietic Protoporphyria, EPP. Retrieved from http://themedicalbiochemistrypage.org/epp.html

4. Casanovs-Gonzalez MJ, Trapero-Marugan M, Jones EA, Moreno-Otero R. (2010). Liver disease and erythropoietic protoporphyria: a concise review. Retreived from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2945483

5. Michael Koch, Constanze Breithaupt, Reiner Kiefersauer, Jörg Freigang, Robert Huber, Albrecht Messerschmidt. (2004). Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394243

6. Vera M. Sellers, Michael K. Johnson, Harry A. Dailey. (1996). Function of the [2Fe-2S] Cluster in Mammalian Ferrochelatase: A Possible Role as a Nitric Oxide Sensor. Retrieved from http://pubs.acs.org/doi/full/10.1021/bi952631p

7. Amy E. Medlock, Michael Carter, Tamara A. Dailey, Harry A. Dailey, and  William N. Lanzilotta. (2009). Product Release Rather than Chelation Determines Metal Specificity for Ferrochelatase. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2771925/

8. Amy E. Medlock, Tamara A. Dailey, Teresa A. Ross, Harry A. Dailey, and William N. Lanzilotta. A π-Helix Switch Selective for Porphyrin Deprotonation and Product Release in Human Ferrochelatase. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2083577/

9.FECH. (2010). Retrieved from http://ghr.nlm.nih.gov/gene/FECH