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Protein Engineering, Vol. 14, No. 11, 939-942, November 2001
© 2001 Oxford University Press

Adjacent cysteine residues as a redox switch

Chiwook Park1,3 and Ronald T. Raines1,2,4

1 Department of Biochemistry and 2 Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, USA

Oxidation of adjacent cysteine residues into a cystine forms a strained eight-membered ring. This motif was tested as the basis for an enzyme with an artificial redox switch. Adjacent cysteine residues were introduced into two different structural contexts in ribonuclease A (RNase A) by site-directed mutagenesis to produce the A5C/A6C and S15C/S16C variants. Ala5 and Ala6 are located in an {alpha}-helix, whereas Ser15 and Ser16 are located in a surface loop. Only A5C/A6C RNase A had the desired property. The catalytic activity of this variant decreases by 70% upon oxidation. The new disulfide bond also decreases the conformational stability of the A5C/A6C variant. Reduction with dithiothreitol restores full enzymatic activity. Thus, the insertion of adjacent cysteine residues in a proper context can be used to modulate enzymatic activity.


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