Portal de Periódicos da CAPES

Solution conformation of lactate dehydrogenase as studied by saturation transfer ESR spectroscopy

1979; Elsevier BV; Volume: 571; Issue: 2 Linguagem: Inglês

10.1016/0005-2744(79)90089-5

1878-1454

Wolfgang E. Trommer, Klaus Glöggler,

Electrochemical sensors and biosensors

Several binary and ternary inhibitor and ‘dead end’ complexes of pig heart lactate dehydrogenase (l-lactate:NAD+ oxidoreductase, EC 1.1.1.27) were studied by saturation transfer ESR spectroscopy by means of an active NAD analog, spin-labeled at N6. The mobility of the spin-label depends on the nature of small molecules bound at the remote catalytic end of the coenzyme. The spin-label was found to serve as a reporter group monitoring the conformation of the peptide loop that is folded down over the active cleft in crystals of ternary complexes. The data suggest a fluctuation of the loop between open and closed forms is solution. The structure of the inhibitor molecules has been correlated with their ability to stabilize a more closed conformation of the loop.