Comparison of the Electron Spin Echo Envelope Modulation (ESEEM) for Human Lactoferrin and Transferrin Complexes of Copper(II) and Vanadyl Ion

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Comparison of the electron spin echo envelope modulation (ESEEM) for human lactoferrin and transferrin complexes of copper(II) and vanadyl ion.

Copper(II) and vanadyl ions were bound to human milk lactoferrin or serum transferrin with carbonate or oxalate as the synergistic anion. Electron spin echo envelope modulation (ESEEM) due to nitrogen of a coordinated histidine imidazole was observed for both the copper and vanadyl complexes. For both metals, the modulation frequencies in the Fourier transforms of the data were similar for the ...

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5- and 6-pulse electron spin echo envelope modulation (ESEEM) of multi-nuclear spin systems.

In 3-pulse ESEEM and the original 4-pulse HYSCORE, nuclei with large modulation depth (k approximately 1) suppress spectral peaks from nuclei with weak modulations (k approximately 0). This cross suppression can impede the detection of the latter nuclei, which are often the ones of interest. We show that two extended pulse sequences, 5-pulse ESEEM and 6-pulse HYSCORE, can be used as experimenta...

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Electron spin echo envelope modulation evidence for carbonate binding to iron(III) and copper(II) transferrin and lactoferrin.

Iron binding to transferrin and lactoferrin requires a synergistic anion, which is carbonate in vivo. The anion is thought to play a key role in iron binding and release. To understand better the iron-carbonate interaction, experiments were performed with iron(III) and copper(II) complexes of human milk lactoferrin and serum transferrin with carbon-13-labeled carbonate. Modulation frequencies w...

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Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM).

The advanced electron paramagnetic resonance (EPR) techniques, electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM) spectroscopies, provide unique insights into the structure, coordination chemistry, and biochemical mechanism of nature's widely distributed iron-sulfur cluster (FeS) proteins. This review describes the ENDOR and ESEEM techniques and then pr...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1989

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)83657-2