Abstract

Recent applications of high-field nmr spectroscopy in the enzymology of biosynthesis are illustrated. The techniques involve the use of 1H-, 3H-, 13C- and 15N-nmr to focus on individual steps of biochemical processes in the formation of natural products and related enzyme-catalyzed events. In the first set of experiments, pulse labeling studies are used to uncover biosynthetic sequences in the porphyrin-corrin pathway. In the second type of nmr experiment, the application of 1H- and 3H-nmr spectroscopy has illuminated the course of certain key biosynthetic steps in the synthesis of porphyrins and beta-lactam antibiotics. These methods have quite general application in biochemical and biological systems. Thirdly, the full magnifying power of the nmr "lens" is used to decipher molecular events during enzyme-catalyzed reactions in solution at subzero temperature and in the solid state.

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