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Structure and function of iron-sulfer cluster biosynthesis proteins and the influence of oxygen ligation

Mansy, Sheref S
http://rave.ohiolink.edu/etdc/view?acc_num=osu1059664189

Abstract Details

2003, Doctor of Philosophy, Ohio State University, Ohio State Biochemistry Program.
Members of the IscU family of proteins are among the most conserved of all protein groups, extending across all three kingdoms of life. IscU is believed to be involved in iron-sulfur cluster delivery to apo iron-sulfur proteins. However, most of the evidence supporting the function of IscU stems from genetic and cellular biological studies. Therefore, we set out to biochemically characterize human, yeast, and prokaryotic IscU proteins. A variety of spectroscopic techniques were used to evaluate IscU including, UV-visible absorption, Mössbauer, near- and far- UV circular dichroism, mass spectrometry, atomic absorption, and nuclear magnetic resonance. Herein we demonstrate that IscU proteins coordinate reductively labile [2Fe-2S]2+ centers and are capable of mediating delivery of intact cluster to apo protein targets. Furthermore, extensive structural and dynamic data of a hyperthermophilic homologue, Thermotoga maritima IscU, revealed that IscU adopts a mobile molten globule-like state that is vastly different from the previously identified ferredoxin-like fold that has thus far been characterized for other metallochaperones. Such a dynamic molecule may allow for the flexibility that is necessary for the multiple roles of Fe-S cluster assembly, and recognition and delivery of that cluster to a target protein. Additionally, we utilized X-ray crystallography to elucidate a high resolution structure of an oxygen ligated [4Fe-4S] high potential iron protein.
James Cowan (Advisor)
272 p.
Chemistry, Biochemistry
Iron-Sulfur Cluster; IscU; NifU; Metallochaperone; High Potential Iron Protein

Recommended Citations

Citations

  • Mansy, S. S. (2003). Structure and function of iron-sulfer cluster biosynthesis proteins and the influence of oxygen ligation [Doctoral dissertation, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1059664189

    APA Style (7th edition)

  • Mansy, Sheref. Structure and function of iron-sulfer cluster biosynthesis proteins and the influence of oxygen ligation. 2003. Ohio State University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1059664189.

    MLA Style (8th edition)

  • Mansy, Sheref. "Structure and function of iron-sulfer cluster biosynthesis proteins and the influence of oxygen ligation." Doctoral dissertation, Ohio State University, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=osu1059664189

    Chicago Manual of Style (17th edition)

osu1059664189
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© 2003, all rights reserved.
This open access ETD is published by The Ohio State University and OhioLINK.
Release 3.2.12