A Nuclear Magnetic Resonance Study of the Metal Binding Sites in Bacitracin

1975 ◽  
Vol 53 (12) ◽  
pp. 1250-1254 ◽  
Author(s):  
Roderick E. Wasylishen ◽  
Moira R. Graham

Carbon-13 nuclear magnetic resonance spectroscopy has been used to identify sites in bacitracin which bind Cu2+ and Mn2+. Results are presented which implicate the free carboxyl groups of the aspartic and glutamic acid residues and the imidazole ring of the histidine residue as metal complexation sites between pH 6 and 8. Evidence is presented which also indicates that the thiazoline ring of bacitracin binds Mn2+. Bacitracin does not bind Cu2+ or Mn2+ at pH values of 2.5 or less.

1987 ◽  
Vol 65 (4) ◽  
pp. 827-832 ◽  
Author(s):  
M. Madalena Caldeira ◽  
M. Luisa Ramos ◽  
Victor M. S. Gil

A proton and carbon-13 nuclear magnetic resonance study is reported on the number, stoichiometry, geometry, and stability of the complexes that form when sodium tungstate or sodium molybdate is mixed with each one of the following α-hydroxyacids in aqueous solution at pH values in the range 3–8: glycolic, lactic, chloro-3- andphenyl-3-lactic, mandelic, and glyceric acids. The predominant complexes have 1:2 composition and pK of formation of the order of −5 to −16.


1971 ◽  
Vol 49 (5) ◽  
pp. 767-776 ◽  
Author(s):  
R. U. Lemieux ◽  
M. A. Barton

Nuclear magnetic resonance spectroscopy has been applied to the study of carbamate formation in solutions of amino acids and peptides in a carbonate-bicarbonate system. The possible conformations of these carbamates are discussed in terms of the n.m.r. data obtained. The n.m.r. parameters are reported for the diastereomers L-alanyl-L or D-phenylalanine and L-phenylalanyl-L or D-alanine and for the dipeptide glycyl-L-phenylalanine and their carbamates. The results are interpreted in terms of preferred rotamers about the Cα—Cβ bond of the phenylalanine residue and a β-type conformation of the peptide chain, wherein the two α-protons lie in the plane of the amide bond. All observations are in agreement with a shorter end to end distance in L,D- compared with L,L-dipeptides.


1988 ◽  
Vol 34 (5) ◽  
pp. 605-612 ◽  
Author(s):  
Yves Bellinger ◽  
François Larher

Glycerol, arabitol and trehalose were the principle solutes detected in cellular extracts of Hansenula anomala, using natural-abundance 13C nuclear magnetic resonance spectroscopy. Only the two polyols accumulated in response to increased salinity, glycerol increase being far greater. Arabitol content also increased with culture age, independently of the presence or absence of salt and in line with the evolution of trehalose content. Glycerol retention potential was 15 times greater for Hansenula than for Saccharomyces cerevisiae. The former displayed the specific property of increasing this capacity in high salt concentrations. Under such conditions its growth was associated with a limited increase in glucose consumption per unit biomass, relative to S. cerevisiae, the salt-sensitive reference yeast. In addition, a polysaccharide, the chemical nature of which was not further characterized, was detected exclusively in the external medium of Hansenula growing in the presence of salt.


1988 ◽  
Vol 66 (10) ◽  
pp. 2601-2604 ◽  
Author(s):  
Photis Dais ◽  
Kevin R. Holme ◽  
Arthur S. Perlin

The binding selectivities of univalent counterions for heparin in the systems Ca2+/M+/HEP, where M+ = Li+, Na+, K+, Cs+, TMA+, have been studied by 13C nuclear magnetic resonance spectroscopy. Chemical shift displacements of the various 13C nuclei of heparin in these systems clearly indicate that the binding selectivity of the polymer for univalent counterions increases with an increase in the radius of the hydrated cation form, namely Li+ > Na+ > K+ > Cs+ > TMA+. An explanation for this binding preference is offered on the basis of electrostatic and entropic terms, whereby the latter is reflected in changes in the hydration volumes of the univalent cations. Differences in the magnitude of these hydration volumes, in relation to the free energies of hydration, may account for a binding selectivity that favours the more highly hydrated ions.


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