Electronic Resource
Springer
Cellular and molecular life sciences
37 (1981), S. 789-798
ISSN:
1420-9071
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Summary The coenzymed-biotin offers in its anionic form to metal ions 3 possible binding sites: the carboxylate group of the valerate side chain, the ureido residue of the 2-imidazolidone ring, and the thioether sulfur of the tetrahydrothiophene ring; the coordinating properties of these groups are summarized and compared. Hydrogen bond formation of the ureido group has also been observed, and hydrogen bonding may possibly be important in biotin-bicarbonate recognition. The aliphatic part of the valeric acid side chain can undergo hydrophobic interactions. Such interactions and/or the stereoselective sulfur-metal ion coordination could be the means for a correct ‘fixation’ of the biotinyl moiety at the surface of a protein, thus creating the active enzyme-substrate complex.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01985645
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