Direct Evidence of Nitrogen Coupling in the Copper(II) Complex of Bovine Serum Albumin by S-Band Electron Spin Resonance Technique

Rakhit, Gopa; Antholine, William E.; Froncisz, Wojciech; Hyde, James S.; Pilbrow, John R.; Sinclair, Geoffrey R.; Sarkar, Bibudhendra

doi:10.1016/0162-0134(85)80015-5

Cited by 57 publications

(42 citation statements)

References 19 publications

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“…In the case of Cu bovine serum albumin [42], both MONOQF, based on perturbation theory, and our modified version of the QPOW program, QPOWFS, based on diagonalization of the spin Hamiltonian at the centre of the spectrum at each orientation, gave closely similar results. This suggests that perturbation theory simulation programs may be relied upon down to a microwave frequency of about 4 GHz for Cu(II) spectra.…”

Section: Some Examples Of Simulations Of S = 1/2 Including Hyperfine supporting

confidence: 55%

EPR spectroscopy of poorly characterized systems: A historical and current view

Pilbrow

1994

Appl. Magn. Reson.

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Modeling of the CW-EPR spectra due to transition metal ions in non-crystalline systems grew in sophistication from the early 1960's until fairly recently. A number of important effects have been introduced into the simulation of CW spectra over the past decade or so.These include allowance for local strain effects, the so-called "g-strain" and correlated "g-A strain", the latter especially important in multifrequency spectroscopy. Limits have been reached in what is reasonable by way of guesses regarding the underlying lineshape function and further information can only be sought via ENDOR or ESEEM experiments in favourable cases. A clear understanding of the simplest way to describe field swept EPR via a master equation derived in the frequency domain will be reviewed in which asymmetric field swept fines sometimes occur naturally as a consequence of the theory. The paper will provide a review of the history of computer simulations and various statistical approaches to correlation effects covering examples as diverse as proteins and glasses. It is hoped that sufficient progress will have been achieved with a new Bruker ESP 380 pulsed spectrometer that some new results can also be reported.

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Section: Some Examples Of Simulations Of S = 1/2 Including Hyperfine supporting

confidence: 55%

EPR spectroscopy of poorly characterized systems: A historical and current view

Pilbrow

1994

Appl. Magn. Reson.

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“…The EPR spectra of Cu II -Ab40 and Cu-HSA are quite different [20,[53][54][55] (Figure 1 be followed by the appearance of a negative peak at 3445 Gauss ( Figure 1) present in Cu II -HSA but not in Cu-Ab40. The development of this peak increased steadily in intensity up to the addition of one equivalent of HSA, where a plateau is reached (Figure 1, inset).…”

Section: Cumentioning

confidence: 95%

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation, Radical Production and Reduces Aβ Toxicity

Perrone¹,

Mothes²,

Vignes³

et al. 2009

ChemBioChem

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Amyloid-beta peptides (Abeta) and the protein human serum albumin (HSA) interact in vivo. They are both localised in the blood plasma and in the cerebrospinal fluid. Among other functions, HSA is involved in the transport of the essential metal copper. Complexes between Abeta and copper ions have been proposed to be an aberrant interaction implicated in the development of Alzheimer's disease, where Cu is involved in Abeta aggregation and production of reactive oxygen species (ROS). In the present work, we studied copper-exchange reaction between Abeta and HSA or the tetrapeptide DAHK (N-terminal Cu-binding domain of HSA) and the consequence of this exchange on Abeta-induced ROS production and cell toxicity. The following results were obtained: 1) HSA and DAHK removed Cu(II) from Abeta rapidly and stoichiometrically, 2) HSA and DAHK were able to decrease Cu-induced aggregation of Abeta, 3) HSA and DAHK suppressed the catalytic HO(.) production in vitro and ROS production in neuroblastoma cells generated by Cu-Abeta and ascorbate, 4) HSA and DAHK were able to rescue these cells from the toxicity of Cu-Abeta with ascorbate, 5) DAHK was more potent in ROS suppression and restoration of neuroblastoma cell viability than HSA, in correlation with an easier reduction of Cu(II)-HSA than Cu-DAHK by ascorbate, in vitro. Our data suggest that HSA is able to decrease aberrant Cu(II)-Abeta interaction. The repercussion of the competition between HSA and Abeta to bind Cu in the blood and brain and its relation to Alzheimer's disease are discussed.

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“…The line widths were determined using parameters for the residual width and the g and A strains, as given in Table 1 for the parameters W , C, and Cz (Rakhit et al, 1985;Pilbrow, 1990). The line widths for the mixed-valence complex incorporates the sum of the three spectra due to the two isotopes for copper.…”

Section: Simulationsmentioning

confidence: 99%

A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase

Antholine

Kastrau

Steffens

et al. 1992

European Journal of Biochemistry

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185

170

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The multicopper proteins, nitrous-oxide reductase (N20R) and cytochrome c oxidase (COX), were investigated by EPR spectroscopy at microwave frequencies 2.4 -35 GHz. Our results support a Cu-Cu interaction in COX and N20R. At least 10 lines in the 2.7-GHz, 12 lines in the 4.6-GHz and 14 lines in the 9.2 GHz spectra were resolved for N20R. Eight copper lines at 2.7 GHz, about ninc lines at 4.6 GHz and about six lines at 9.2 G H L were resolved for COX. Simulations of the EPR spectra were consistent with most of the resonances of the multiline spectra, including regions in the center of the spectra where overlap of the three seven-line patterns is proposed. These simulations indicated that Cu-Cu interaction, in a mixed-valence [Cu(l.5). . .Cu(l.5)], S = site is consistent with, if not proof of, the unusual spectral features observed for N 2 0 R and COX.Nitrous-oxide reductase (N20R) is the terminal electron acceptor in a respiratory chain converting N 2 0 to N2 in denitrifying bacteria: N 2 0 + 2H' + 2e-N2 + H 2 0 .

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Direct Evidence of Nitrogen Coupling in the Copper(II) Complex of Bovine Serum Albumin by S-Band Electron Spin Resonance Technique

Cited by 57 publications

References 19 publications

EPR spectroscopy of poorly characterized systems: A historical and current view

EPR spectroscopy of poorly characterized systems: A historical and current view

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation, Radical Production and Reduces Aβ Toxicity

A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase

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