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Enzyme Research

Researchers from University of Rome, Department of Biology detail findings in enzyme research

Published in Cancer Weekly, February 2nd, 2010

Scientists discuss in 'Inactivation of cytochrome c oxidase by mutant SOD1s in mouse motoneuronal NSC-34 cells is independent from copper availability but is because of nitric oxide' new findings in enzyme research. According to recent research from Rome, Italy, "The copper-enzyme cytochrome c oxidase (Cytox) has been indicated as a primary molecular target of mutant copper, zinc superoxide dismutase (SOD1) in familial amyotrophic lateral sclerosis (fALS); however, the mechanism underlying its inactivation is still unclear. As the toxicity of mutant SOD1s could arise from their selective recruitment to mitochondria, it is conceivable that they might compete with Cytox for the mitochondrial...

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