Magnetic circular dichroism studies of iron(ii) binding to human calprotectin

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

Calprotectin (CP) is an abundant metal-chelating protein involved in host defense, and the ability of human CP to bind Fe(ii) in a calcium-dependent manner was recently discovered. In the present study, near-infrared magnetic circular dichroism spectroscopy is employed to investigate the nature of Fe(ii) coordination at the two transition-metal-binding sites of CP that are a His3Asp motif (site...

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin† †Electronic supplementary information (ESI) available: Sample details and supplemental magnetic circular dichroism spectra. See DOI: 10.1039/c6sc03487j Click here for additional data file.

Adenine binding to glutamate dehydrogenase: Natural and magnetic circular dichroism studies.

In the study of a nicotinamide adenine dinucleotide dependent dehydrogenase, one meets, among others, the following problems: are both aromatic rings of the nucleotide necessary for the binding to the enzyme and for the catalysis; which is their respective role; how are they interacting with the protein and with one another? In the case of lactate dehydrogenase, crystallographic data are availa...

Applications of Magnetic Circular Dichroism for Studies of Organic Molecules

Magnetic circular dichroism (MCD) spectroscopy provides extended information about molecular electronic structure and transitions. Because the chirality is induced by static magnetic field it can also be used for non-chiral compounds. However, interpretation of the spectra is difficult, and precise computations using quantum mechanical approaches were implemented in publicly available software ...

Magnetic circular dichroism and cobalt(II) binding equilibrium studies of Escherichia coli methionyl aminopeptidase.

Equilibrium dialysis of methionyl aminopeptidase from Escherichia coli (EcMetAP) monitored by atomic absorption spectrometry and magnetic circular dichroism (MCD) shows that the enzyme binds up to 1.1 +/- 0.1 equiv of Co(2+) in the metal concentration range likely to be found in vivo. The dissociation constant, K(d), is estimated to be between 2.5 and 4.0 microM. Analysis of the temperature and...