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Synthesis and properties of new coenzyme mimics based on the artificial coenzyme CL4
Author(s) -
Ansell Richard J.,
Small David A. P.,
Lowe Christopher R.
Publication year - 1999
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(199901/02)12:1<45::aid-jmr374>3.0.co;2-9
Subject(s) - coenzyme a , cofactor , chemistry , coenzyme q – cytochrome c reductase , biochemistry , enzyme , reductase , cytochrome c , mitochondrion
We have previously shown that a range of nicotinamide containing ‘biomimetic coenzymes’ function as active analogues of NAD + in the oxidation of alcohols by horse liver alcohol dehydrogenase (HLADH), despite their apparently astonishing lack of structural similarity to the natural coenzyme. The simplest structure as yet shown to exhibit activity is the biomimetic coenzyme CL4. To investigate the effect of the structure of this truncated artificial coenzyme on its activity, a range of close structural analogues of CL4 were designed, synthesized and characterized. The electrochemical reduction potentials of the analogues were strongly influenced by the nature of the groups attached to the pyridine ring. All of the analogues could be chemically reduced using sodium borohydride, to give compounds with altered UV‐visible absorption and fluorescence properties. An HPLC‐based assay suggested that two of the new analogues were coenzymically active in the oxidation of butan‐1‐ol by HLADH, with one displaying a significantly higher activity than CL4. The results demonstrate which features of the structures of the coenzymes lead to desirable electrochemical and spectroscopic properties, but suggest that the structural requirements for a functional coenzyme are quite stringent. These observations may be used to design an artificial coenzyme which combines the best features of those studied so far. Copyright Copyright © 1999 John Wiley & Sons, Ltd.