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Mechanism of Fe-S cluster biosynthesis: the [2Fe-2S] IscU as a model scaffold

Nuth, Manunya
http://rave.ohiolink.edu/etdc/view?acc_num=osu1092856116

Abstract Details

2004, Doctor of Philosophy, Ohio State University, Biochemistry.
Of the transition metals, iron is the metal of choice for cells (with the exception of a few Lactobacillus species) found mainly in heme and Fe-S cofactors. However despite being an essential mineral, iron has the ability to activate dioxygen toward the formation of reactive oxygen species (ROS) capable of damaging biomolecules. As such, maintenance of iron concentrations is crucial. Reconstitution of Fe-S proteins is facile and is comprised of simply incubating the apo protein with excess inorganic iron salts and sulfides in the presence of a reductant such as β-mercaptoethanol or dithiothreitol (DTT). Because free iron and sulfide are cellulary toxic, accessory proteins are undoubtedly essential for provisions of iron and sulfur equivalents for the maturation of Fe-S proteins. Since first characterized in the 1960s, only recent progress in the last decade has provided insights into understanding Fe-S biosynthesis. Three such systems are known: 1) nif – gene products involved in the maintenance of nitrogenase biosynthesis; 2) isc – homologous to nif and found in both bacteria and eukaryotes; and 3) suf – implicated to be redundant to isc. In this study, IscU serves as a platform for understanding the mechanism of [2Fe-2S] cluster assembly utilizing its substrate IscS, a desulfurase that catalyzes the decomposition of L-Cys to Ala and sulfur equivalents for the IscU scaffold. Both proteins are gene products of the isc (iron sulfur cluster) operon, the topic of the current work.
James Cowan (Advisor)
Chemistry, Biochemistry
Fe-S; iron-sulfur; IscU; IscS; NifS

Recommended Citations

Citations

  • Nuth, M. (2004). Mechanism of Fe-S cluster biosynthesis: the [2Fe-2S] IscU as a model scaffold [Doctoral dissertation, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1092856116

    APA Style (7th edition)

  • Nuth, Manunya. Mechanism of Fe-S cluster biosynthesis: the [2Fe-2S] IscU as a model scaffold. 2004. Ohio State University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1092856116.

    MLA Style (8th edition)

  • Nuth, Manunya. "Mechanism of Fe-S cluster biosynthesis: the [2Fe-2S] IscU as a model scaffold." Doctoral dissertation, Ohio State University, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=osu1092856116

    Chicago Manual of Style (17th edition)

osu1092856116
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© 2004, all rights reserved.
This open access ETD is published by The Ohio State University and OhioLINK.