Solution behavior and complete sup 1 H and sup 13 C NMR assignments of the coenzyme B sub 12 derivative (5 prime -deoxyadenosyl)cobinamide using modern 2D NMR experiments, including 600-MHz sup 1 H NMR data

Journal Article · Wed Feb 15 00:00:00 EST 1989 · Journal of the American Chemical Society; (USA)

DOI:https://doi.org/10.1021/ja00186a051· OSTI ID:5117069

Pagano, T G; Yohannes, P G; Marzilli, L G ^[1]; Hay, B P; Scott, J R; Finke, R G ^[2]

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1. Emory Univ., Atlanta, GA (USA)
2. Univ. of Oregon, Eugene (USA)

Two-dimensional (2D) NMR methods have been used to assign completely the {sup 1}H and {sup 13}C NMR spectra of the (5{prime}-deoxyadenosyl)cobinamide cation (AdoCbi{sup +}) in D{sub 2}O. Most of the {sup 1}H spectral assignments were made by using 2D homonuclear shift correlation spectroscopy (COSY), homonuclear Hartmann-Hahn spectroscopy (HOHAHA), absorption-mode (phase sensitive) 2D nuclear Overhauser effect (NOE) spectroscopy, and spin-locked NOE spectroscopy (also called ROESY, for rotating-frame Overhauser enhancement spectroscopy). Most of the protonated carbon resonances were assigned by using {sup 1}H-detected heteronuclear multiple-quantum coherence (HMQC) spectroscopy. The nonprotonated carbon resonances, as well as the remaining unassigned {sup 1}H and {sup 13}C NMR signals, were assigned from long-range {sup 1}H-{sup 13}C connectivities determined from {sup 1}H-detected multiple-bond heteronuclear multiple-quantum coherence spectroscopy (HMBC). Comparison of the {sup 13}C chemical shifts and {sup 1}H NOEs of AdoCbi{sup +} with those of coenzyme B{sup 12} ((5{prime}-deoxyadenosyl)cobalamin) and its benzimidazole-protonated, base-off form indicates that the electronic properties and structure of AdoCbi{sup +} are similar to that of coenzyme B{sup 12} in the protonated, base-off form. The {sup 13}C chemical shifts of most of the carbons of AdoCbi{sup +} do not vary significantly from those of base-off, benzimidazole-protonated coenzyme B{sup 12}, indicating that the electronic environment of the corrin ring is also similar in both compounds. However, significant differences in the chemical shifts of some of the corresponding carbons of the b, d, e, and f corrin side chains in AdoCbi{sup +} and in base-off, benzimidazole-protonated coenzyme B{sub 12} indicate that the positions of these side chains may be different in AdoCbi{sup +} compared to base-off coenzyme B{sup 12}.

• OSTI ID: 5117069
• Journal Information: Journal of the American Chemical Society; (USA), Vol. 111:4; ISSN 0002-7863
• Country of Publication: United States
• Language: English

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37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
COENZYMES
MOLECULAR STRUCTURE
HEAVY WATER
ISOTOPE EFFECTS
VITAMIN B GROUP
CARBON 13
EXPERIMENTAL DATA
NMR SPECTRA
PROTONS
SOLVENT PROPERTIES
BARYONS
CARBON ISOTOPES
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ELEMENTARY PARTICLES
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FERMIONS
HADRONS
HYDROGEN COMPOUNDS
INFORMATION
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LIGHT NUCLEI
NUCLEI
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OXYGEN COMPOUNDS
SPECTRA
STABLE ISOTOPES
VITAMINS
WATER
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400202 - Isotope Effects
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