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Table I. Data for Bimolecular H/D Exchange and Termolecular Addition of D2 to (r;4-C4H6)Fe(CO)~• (m/z 138)" % decay of m/z 138 % of product ion signals (C4H5D)-Fe(CO)™• m/z 139 (C4H4D2)-Fe(CO)™• m/z 140 (C4H3D3)-Fe(CO)™• m/z 141 (C4H2D4)-Fe(CO)'• + (C4H6)-Fe(CO)(D)2™• m/z 142 (C4H5D)-Fe(CO)(D)2™• m/z 143 (C4H4D2)-Fe(CO)(D2)-• m/z 144 (C4H3D3)-Fe(CO)(D)2-• m/z 145 (C4H2D4)-Fe(CO)(D)f.

Electrochemical reduction of lysozyme disulfide bonds was achieved at pH between 10 and 11. Below pH 10, no disulfide bond cleavage was observed. At pH higher than 12, the cleavage of disulfide bonds is essentially due to hydrolysis. The addition of denaturant considerably enhanced the performance of the electrochemical device.

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