Related Articles31P-NMR of free and protein-bound molybdopterin guanine dinucleotide.
Biofactors. 1992 Jan;3(3):197-200
Authors: Bastian NR, Johnson JL, Rajagopalan KV
Molybdopterin guanine dinucleotide was studied by 31P-NMR in the free, iodoacetamide derivatized form [di(carboxamidomethyl)molybdopterin] and in the native state in the dimethyl sulfoxide reductase from Rhodobacter sphaeroides. The spectra confirm the presence of a pyrophosphate moiety in the cofactor molecule. Comparison of the spectrum of the free pterin with that of the protein-bound cofactor reveals a substantial upfield shift of the 31P resonances in the enzyme-bound form with respect to the free form. This shift is attributed to differences in the bond and torsional angles of the phosphates. The spectrum of the protein suggests significant coupling between the two phosphorus nuclei with coupling constants of approximately 200 Hz. Comparison of the 31P-NMR spectra of molybdopterin guanine dinucleotide and flavin adenine dinucleotide suggests that the two cofactors have similar conformations in both their free and protein-bound forms.
[NMR paper] Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
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J Biomol NMR. 2005 Jul;32(3):235-41
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Biochemistry. 2002 Feb 5;41(5):1457-63
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J Mol Biol. 1999 Aug 20;291(3):521-30
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31P-NMR of free and protein-bound molybdopterin guanine dinucleotide.
Linear Mode
