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Metallo-?-lactamases: two binding sites for one catalytic metal ion?
During the past few years the results from molecular biological, biochemical, chemical, physical and theoretical approaches expanded the knowledge about metallo-β-lactamases considerably. The main reason for the attracted interest is a persisting medical problem. Bacteria expressing metallo-β-lactam...
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Published in: | Cellular and molecular life sciences : CMLS 2004-11, Vol.61 (22), p.2827-2839 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
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Summary: | During the past few years the results from molecular biological, biochemical, chemical, physical and theoretical approaches expanded the knowledge about metallo-β-lactamases considerably. The main reason for the attracted interest is a persisting medical problem. Bacteria expressing metallo-β-lactamases can be resistant to treatment with all the known β-lactam antibiotics, and they are additionally invulnerable to combined treatment with inhibitors for the wider-spread serine-β-lactamases. However, clinically useful inhibitors for metallo-β-lactamases are not yet available. In spite of the rapidly expanding knowledge base a central question is still controversially discussed: is it the mononuclear, the binuclear or the metal-free state which might serve as the physiologically relevant target for inhibitor design? A summary of the present views of the roles and coordination geometries of metal ion(s) in metallo-β-lactamases is combined with a discussion of the possibly variable metal ion content under physiological conditions.[PUBLICATION ABSTRACT] |
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ISSN: | 1420-682X 1420-9071 |
DOI: | 10.1007/s00018-004-4214-9 |