Abstract

Sulfite Reductase Hemoprotein (SiRHP) constitutes the catalytic subunit of the multicomponet enzyme complex Sulfite Reductase. Sulfite Reductase is responsible for the six electron reduction of sulfite to sulfide in the biological assimilation of sulfur. When supplied with artificial electron donors, SiRHP, a 64 KDa monomer, is fully capable of the reductive chemistry performed by the complex. The hemoprotein subunit utilizes a unique assembly of cofactors to transfer electrons to substrate. The structure of the oxidized enzyme is currently being built and refined. Atomic resolution information on this enzyme in its various complexed and reduced forms should lend great insight into the chemistry involved in the biological reduction of low molecular weight compounds.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-17
Application #
5222695
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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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
Vickers, Chelsea; Liu, Feng; Abe, Kento et al. (2018) Endo-fucoidan hydrolases from glycoside hydrolase family 107 (GH107) display structural and mechanistic similarities to ?-l-fucosidases from GH29. J Biol Chem 293:18296-18308
Nguyen, Phong T; Lai, Jeffrey Y; Lee, Allen T et al. (2018) Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP Binding Cassette (ABC) transporter. Proc Natl Acad Sci U S A 115:E10596-E10604
Dods, Robert; Båth, Petra; Arnlund, David et al. (2017) From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography. Structure 25:1461-1468.e2
de Vries, Robert P; Tzarum, Netanel; Peng, Wenjie et al. (2017) A single mutation in Taiwanese H6N1 influenza hemagglutinin switches binding to human-type receptors. EMBO Mol Med 9:1314-1325

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