title: Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics.
abstract: Peroxiredoxins (Prx) are ubiquitous enzymes that reduce peroxides as part of antioxidant defenses and redox signaling. While Prx catalytic activity and sensitivity to hyperoxidative inactivation depend on their dynamic properties, there are few examples where their dynamics has been characterized by NMR spectroscopy. Here, we provide a foundation for studies of the solution properties of peroxiredoxin Q from the plant pathogen Xanthomonas campestris (XcPrxQ) by assigning the observable (1)H(N), (15)N, (13)C(α), (13)C(β), and (13)C' chemical shifts for both the reduced (dithiol) and oxidized (disulfide) states. In the reduced state, most of the backbone amide resonances (149/152, 98 %) can be assigned in the XcPrxQ (1)H-(15)N HSQC spectrum. In contrast, a remarkable 51 % (77) of these amide resonances are not visible in the (1)H-(15)N HSQC spectrum of the disulfide state of the enzyme, indicating a substantial change in backbone dynamics associated with the formation of an intramolecular C48-C84 disulfide bond.
authors.affiliation: Earth and Biological Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA, 99352, USA. garry.buchko@pnnl.gov.
authors.forename: Garry W
authors.initials: GW
authors.lastname: Buchko
authors.affiliation: Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, 97331, USA.
authors.forename: Arden
authors.initials: A
authors.lastname: Perkins
authors.affiliation: Department of Biochemistry, Wake Forest School of Medicine, Winston-Salem, NC, 27157, USA.
authors.forename: Derek
authors.initials: D
authors.lastname: Parsonage
authors.affiliation: Department of Biochemistry, Wake Forest School of Medicine, Winston-Salem, NC, 27157, USA.
authors.forename: Leslie B
authors.initials: LB
authors.lastname: Poole
authors.affiliation: Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, 97331, USA. karplusp@science.oregonstate.edu.
authors.forename: P Andrew
authors.initials: PA
authors.lastname: Karplus
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D004220:Disulfides / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D054464:Peroxiredoxins / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000378:metabolism; D016959:Xanthomonas campestris / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D004220:Disulfides; D013438:Sulfhydryl Compounds; D054464:Peroxiredoxins
keywords: Conformational change; Drug design; Peroxidase; Plant diseases