Cysteine pKa Values for the Bacterial Peroxiredoxin AhpC
نویسندگان
چکیده
منابع مشابه
Cysteine pK(a) values for the bacterial peroxiredoxin AhpC.
Salmonella typhimurium AhpC is a founding member of the peroxiredoxin family, a ubiquitous group of cysteine-based peroxidases with high reactivity toward hydrogen peroxide, organic hydroperoxides, and peroxynitrite. For all of the peroxiredoxins, the catalytic cysteine, referred to as the peroxidatic cysteine (C(P)), acts as a nucleophile in attacking the peroxide substrate, forming a cysteine...
متن کاملSubstrate specificity and redox potential of AhpC, a bacterial peroxiredoxin.
Typical 2-Cys peroxiredoxins (Prxs) are ubiquitous peroxidases that are involved in peroxide scavenging and/or the regulation of peroxide signaling in eukaryotes. Despite their prevalence, very few Prxs have been reliably characterized in terms of their substrate specificity profile and redox potential even though these values are important for gaining insight into physiological function. Here,...
متن کاملAnalysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin.
Peroxiredoxins (Prxs) make up a ubiquitous class (proposed EC 1.11.1.15) of cysteine-dependent peroxidases with roles in oxidant protection and signal transduction. An intriguing biophysical property of typical 2-Cys Prxs is the redox-dependent modulation of their oligomeric state between decamers and dimers at physiological concentrations. The functional consequences of this linkage are unknow...
متن کاملEstimating pKa values for pentaoxyphosphoranes.
pKa values are estimated independently, by two entirely different methods, for the ionizations of the apical and equatorial OH groups of two representative hydroxyphosphoranes. A bond length-pKa correlation based on crystal structures of cyclohexanol derivatives gives values of 13.5 +/- 1.5 and 8.62 +/- 1.87, respectively, for the apical and equatorial OH groups of tetracyclohexyloxyhydroxyphos...
متن کاملSupplemental Data: Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase
METHODS Spectral and Anaerobic Measurements. All absorbance spectra and anaerobic titrations employed the thermostatted Milton Roy Spectronic 3000 diode array spectrophotometer. The oxidoreductase and DTNB assays were performed on a thermostatted Applied Photophysics DX.17MV stopped-flow spectrofluorometer. The molar extinction coefficients of the proteinbound FAD at 448 or 449 nm were determin...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemistry
سال: 2008
ISSN: 0006-2960,1520-4995
DOI: 10.1021/bi801718d