2-DIMENSIONAL NMR-STUDIES OF NATIVE COENZYME-F430

Modern two-dimensional (2D) NMR spectroscopic methods are used to determine signal assignments and structural features of the recently discovered nickel(II)-containing coenzyme F430. This is the first detailed 1H and 13C NMR study of the native form of coenzyme F430. With the use of COSY, HOHAHA, NOESY, and ROESY 1H-1H correlated spectroscopies in combination with HMQC and HMBC 1H-13C correlated spectroscopies, signal assignments were made for all carbon atoms and nonexchangeable protons. The data confirm 16 of the 21 specific 13C NMR signal assignments made earlier for native F430 by classical ID NMR methods and provide assignment (or reassignment) of the remaining carbon atoms. The NMR signal assignments reported here are in good agreement with the partial assignments reported previously for the pentamethyl ester derivative of F430 (F430M) in CD2C12 solution. In addition, long-range through-bond 1H-13C connectivities confirm aspects of the F430 structurededuced from studies of F430M by traditional spectroscopic and chemical methods. © 1990, American Chemical Society. All rights reserved.