Metal-binding region FALS

In contrast, metal and stractural analyses of the second group of FALS mutants show that these proteins are fully capable of binding metals and retain enzymatic activity, if they are properly folded. Thus, they have been termed wild-type-like. It is postulated that these mutants have higher prooxidant activity (possibly via bicarbonate-mediated inactivation, see Scheme 2). Self-inactivation could lead to metal loss and similar aggregation effects described for the metal-binding-region mutants. 

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