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FEBS Lett. 1997 Jan 3;400(2):155-7.

Site-specific introduction of an electroactive label into a non-electroactive enzyme (beta-lactamase I).

Author information

1
New Chemistry Laboratory, University of Oxford, UK.

Abstract

A cysteine residue was introduced close to the active site of beta-lactamase I by site-directed mutagenesis to replace tyrosine-105 and was subsequently modified with an electroactive SH-specific reagent, N-(2-ferrocene-ethyl)maleimide. The resulting modified enzyme became electroactive, showing good quasireversible electrochemistry which was characteristic of the attached ferrocene moiety while retaining its specific enzymatic activity. In the presence of a suicide substrate, 6beta-iodopenicillanic acid, the redox potential shifted +20 mV suggesting that the label was sensitive to changes in the active site of the enzyme.

PMID:
9001388
DOI:
10.1016/s0014-5793(96)01373-7
[Indexed for MEDLINE]
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