Title : Cu,Zn-superoxide dismutase-driven free radical modifications: copper- and carbonate radical anion-initiated protein radical chemistry.

Pub. Date : 2009 Jan 1

PMID : 18764780






2 Functional Relationships(s)
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1 In the presence of (bi)carbonate and DTPA (diethylenetriaminepenta-acetic acid) (to suppress copper chemistry), CO(*-) produced distinct radical sites in both SOD1 and HSA, which caused protein aggregation without causing protein fragmentation. Bicarbonates superoxide dismutase 1 Homo sapiens
2 Finally, we propose a biochemical mechanism to explain CO(*-) production from CO2, enhanced protein radical formation and protection by (bi)carbonate against H2O2-induced fragmentation of the SOD1 active site. Bicarbonates superoxide dismutase 1 Homo sapiens