Trypsin inhibition by ferrocene | Zendy

Zoran Kukrić | Zendy; Mirjana Žabić | Zendy

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Trypsin inhibition by ferrocene

Author(s) -

Zoran Kukrić,

Mirjana Žabić

Publication year - 2005

Publication title -

acta periodica technologica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.134

H-Index - 15

eISSN - 2406-095X

pISSN - 1450-7188

DOI - 10.2298/apt0536203k

Subject(s) - ferrocene , trypsin , cyclopentadienyl complex , chemistry , enzyme , active site , stereochemistry , arginine , biochemistry , amino acid , catalysis , electrode , electrochemistry

Many transition metals and their complexes show inhibitory effect on someproteolytic enzymes, including trypsin. Their inhibitory activity is based on the direct binding to the active site of trypsin, mimicking formation of a five-coordinate transition state required for the reaction. The influence of ferrocene on trypsin activity using N-α-benzoyl-DL-arginine p-nitroanilide as a substrate was investigated. Ferrocene was selected as a potential inhibitor because it belongs to the family oforganometallic, so called "sandwich " compounds, and its cyclopentadienyl rings might have an appropriate geometry. It was found that ferrocene decreases trypsin activity and the K. for ferrocene was found to be 39.8

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