2003
DOI: 10.1021/bi0205799
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Catecholase Activity Associated with Copper-S100B

Abstract: This study addresses the spectroscopic properties and reactivity associated with the copperloaded form of S100B isolated from bovine brain. Copper(II)-S100B displays EPR features typical of a type II copper center and is shown here to exhibit catecholase activity, the two-electron oxidation of catechols. The steady-state kinetics associated with the oxidation of several catecholamines has been probed in order to further characterize this activity. The evidence provided indicates that the catecholase chemistry … Show more

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Cited by 26 publications
(7 citation statements)
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“…Specifically, it is known that calcium binding to S100 proteins triggers conformational changes that expose a hydrophobic cleft that is crucial to interaction with partners to their activation, regulation and signaling functions. Several S100 proteins also bind zinc and copper, which interestingly are highly abundant in senile plaques (Heizmann et al, 2002; Senior et al, 2003; Maynard et al, 2005). A few S100 proteins are also found as heterodimers, including S100A8/A9 (Teigelkamp et al, 1991), S100B/A1 (Garbuglia et al, 1999) and S100A6/B (Yang et al, 1999).…”
Section: The S100 Protein Familymentioning
confidence: 99%
“…Specifically, it is known that calcium binding to S100 proteins triggers conformational changes that expose a hydrophobic cleft that is crucial to interaction with partners to their activation, regulation and signaling functions. Several S100 proteins also bind zinc and copper, which interestingly are highly abundant in senile plaques (Heizmann et al, 2002; Senior et al, 2003; Maynard et al, 2005). A few S100 proteins are also found as heterodimers, including S100A8/A9 (Teigelkamp et al, 1991), S100B/A1 (Garbuglia et al, 1999) and S100A6/B (Yang et al, 1999).…”
Section: The S100 Protein Familymentioning
confidence: 99%
“…A majority of the selected metals e.g., Na, K, Mg, Ca, Zn, Cu are essential macroand microelements for living organisms. Some metal ions are required for the activity of appropriate enzymes [60][61][62][63][64][65][66][67][68][69].…”
Section: Introductionmentioning
confidence: 99%
“…At pH 6.5, these sites are defined by His15 and His25 from one monomer, and His85 and Glu89 from the other monomer. 47,48 Both of these sites coordinate Zn(II) and Cu(II).…”
Section: Selection and Preparation Of S100 Proteinsmentioning
confidence: 99%
“…2b). Although S100B binds transition metal ions, including Cu(II) and Zn(II), 45,47,48,73 the protein may not be able to tune the aggregation of metal-Aβ 40 . Similar to CP-Ser and CP-Ser ∆∆ , neither S100B nor S100B ∆ could interfere with fibrillization of metal-free Aβ 42 and metal-Aβ 42 ( Fig.…”
Section: Effect Of S100b On Metal-free and Metal-induced Aβ β β β Aggmentioning
confidence: 99%