دورية أكاديمية
أعرض في EDS

Pulsed EPR investigations of the Mo(V) centers of the R55Q and R55M variants of sulfite dehydrogenase from Starkeya novella.

التفاصيل البيبلوغرافية
العنوان: Pulsed EPR investigations of the Mo(V) centers of the R55Q and R55M variants of sulfite dehydrogenase from Starkeya novella.
المؤلفون: Rapson TD; Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, QLD, 4072, Australia., Astashkin AV, Johnson-Winters K, Bernhardt PV, Kappler U, Raitsimring AM, Enemark JH
المصدر: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [J Biol Inorg Chem] 2010 May; Vol. 15 (4), pp. 505-14. Date of Electronic Publication: 2010 Jan 19.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Germany NLM ID: 9616326 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-1327 (Electronic) Linking ISSN: 09498257 NLM ISO Abbreviation: J Biol Inorg Chem Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Berlin : Springer, c1996-
مواضيع طبية MeSH: Amino Acid Substitution* , Genetic Variation* , Molybdenum*, Alphaproteobacteria/*enzymology , Mutant Proteins/*chemistry , Sulfite Dehydrogenase/*chemistry, Catalytic Domain ; Electron Spin Resonance Spectroscopy ; Electron Transport ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Kinetics ; Ligands ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Mutation ; Sulfite Dehydrogenase/genetics ; Sulfite Dehydrogenase/metabolism
مستخلص: Continuous-wave and pulsed electron paramagnetic resonance (EPR) spectroscopy have been used to characterize two variants of bacterial sulfite dehydrogenase (SDH) from Starkeya novella in which the conserved active-site arginine residue (R55) is replaced by a neutral amino acid residue. Substitution by the hydrophobic methionine residue (SDH(R55M)) has essentially no effect on the pH dependence of the EPR properties of the Mo(V) center, even though the X-ray structure of this variant shows that the methionine residue is rotated away from the Mo center and a sulfate anion is present in the active-site pocket (Bailey et al. in J Biol Chem 284:2053-2063, 2009). For SDH(R55M) only the high-pH form is observed, and samples prepared in H(2)(17)O-enriched buffer show essentially the same (17)O hyperfine interaction and nuclear quadrupole interaction parameters as SDH(WT) enzyme. However, the pH dependence of the EPR spectra of SDH(R55Q), in which the positively charged arginine is replaced by the neutral hydrophilic glutamine, differs significantly from that of SDH(WT). For SDH(R55Q) the blocked form with bound sulfate is generated at low pH, as verified by (33)S couplings observed upon reduction with (33)S-labeled sulfite. This observation of bound sulfate for SDH(R55Q) supports our previous hypothesis that sulfite-oxidizing enzymes can exhibit multiple pathways for electron transfer and product release (Emesh et al. in Biochemistry 48:2156-2163, 2009). At pH > or = 8 the high-pH form dominates for SDH(R55Q).
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معلومات مُعتمدة: S10RR020959 United States RR NCRR NIH HHS; R01 GM037773-34 United States GM NIGMS NIH HHS; GM-37773 United States GM NIGMS NIH HHS; R01 GM037773-33 United States GM NIGMS NIH HHS; R01 GM037773 United States GM NIGMS NIH HHS; S10 RR020959 United States RR NCRR NIH HHS; S10 RR020959-01 United States RR NCRR NIH HHS
المشرفين على المادة: 0 (Ligands)
0 (Mutant Proteins)
81AH48963U (Molybdenum)
EC 1.8.2.1 (Sulfite Dehydrogenase)
تواريخ الأحداث: Date Created: 20100120 Date Completed: 20100701 Latest Revision: 20211020
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC2875948
DOI: 10.1007/s00775-009-0619-0
PMID: 20084533
قاعدة البيانات: MEDLINE
الوصف
تدمد:1432-1327
DOI:10.1007/s00775-009-0619-0