Cu, Zn Superoxide dismutase: distorted active site binds substrate without significant energetic cost

Branco,

doi:10.1007/s00214-005-0024-x

Cited by 1 publication

(1 citation statement)

References 45 publications

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“…It has been reported that a 10 kDa fragment including the active center and other fragments (5 kDa) of SOD can be formed by H 2 O 2 addition as a result of the fragmentation of SOD . The active site contains four His residues with Cu 2+ and Zn 2+ , catalyzing the dismutation of the toxic superoxide radical into molecular oxygen and hydrogen peroxide without a significant energy cost . A UV spectral analysis of the fragmented SOD separated by HPLC indicated that the fragmented SOD contains histidine residues or other residues with aromatic rings (data not shown).…”

Section: Resultsmentioning

confidence: 99%

Liposome-Recruited Activity of Oxidized and Fragmented Superoxide Dismutase

et al. 2007

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The peptide fragment of H2O2-treated Cu,Zn-superoxide dismutase (SOD) was found to be reactivated with liposomes prepared by 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC). The fragmentation of SOD was observed by 2 mM H2O2 treatment as well as by SOD inactivation and the loss of an alpha-helix in the neighborhood of its activity center. The H2O2-treated SOD, which lost its activity at different incubation times, was dramatically reactivated only by adding POPC liposomes, resulting in 1.3-2.8 times higher enzymatic activity. The ultrafiltration analysis of H2O2-treated SOD co-incubated with liposomes shows that some specific peptide fragments of the oxidized SOD can interact with POPC liposomes. A comparison of the fractions detected in reverse-phase chromatography shows that specific SOD fragments are able to contribute to the reactivation of oxidized and fragmented SOD in the presence of POPC liposomes. The liposomes can recruit the potentially active fragment of SOD among the lethally damaged SOD fragments to elucidate the antioxidative function.

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Section: Resultsmentioning

confidence: 99%