Abstract
Re-examination of the structure of pyridine coenzymes in solution by use of the 220-MHz high-frequency nuclear magnetic resonance spectrometer indicates that there is primarily one folded structure that is in rapid equilibrium with an open form. Reduced DPN(+) and reduced analogs of DPN(+) exist predominantly with the B side of the dihydropyridine ring folded against the adenine moiety. (The oxidized coenzymes appear to exist in the same folded structure.) Furthermore, the ribose protons undergo very little conformational change upon reduction of the pyridine ring; this observation strongly suggests a considerable similarity between the folded forms of the oxidized and reduced coenzymes. A model of the folded structure is presented.