Abstract

Pyrococcus furiosus ferredoxin is unique among ferredoxins in having a single Fe 4S4 cluster with one iron possessing non-sulfur coordination. An unusual feature of the protein is the ease with which the cluster can lose this iron to form a Fe 3S4 ferredoxin. The Fe 3S4 ferredoxin can readily be reconstituted with Fe to reform the native Fe4 S4 cluster, or alternatively with other metals ions to generate a mixed-metal iron sulfur cluster MFe3S4. Mixed metal iron sulfur clusters comprise a very important class of metalloprotein active sites and are of considerable interest. We propose to use XAS to systematically probe the electronic and physical structure of the different MFe 3S4 clusters in Pyrococcus furiosus ferredoxin.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-17
Application #
5222818
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
17
Fiscal Year
1996
Total Cost
Indirect Cost

  Publications

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Pluvinage, Benjamin; Grondin, Julie M; Amundsen, Carolyn et al. (2018) Molecular basis of an agarose metabolic pathway acquired by a human intestinal symbiont. Nat Commun 9:1043
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Yoshizawa, Takuya; Ali, Rustam; Jiou, Jenny et al. (2018) Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. Cell 173:693-705.e22
Hettle, Andrew; Fillo, Alexander; Abe, Kento et al. (2017) Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of ?-1,3-glucan. J Biol Chem 292:16955-16968
Oberthuer, Dominik; Knoška, Juraj; Wiedorn, Max O et al. (2017) Double-flow focused liquid injector for efficient serial femtosecond crystallography. Sci Rep 7:44628

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