RESUMO
Adsorption of gases on the surface of all-bcc (Fe/Co)N superlattices drives the in-plane, 90° magnetization rotation of the bulk-like Fe(110) supporting ferromagnet. Both experimental and theoretical results prove that terminating the surface of (Fe/Co)N superlattices either by Co or by Fe switches "ON" or "OFF" the spin orientation sensitivity to adsorption. Results indicate that purely surface limited adsorption processes strongly modify the magnetic anisotropy of the entire (Fe/Co)N superlattice, which acts as a kind of "artificial" surface of the bulky Fe(110) ferromagnet. Such an artificial magnetic surface anisotropy concept not only enhances the surface contribution in classical surface-bulk competition but also provides its additional chemical sensitivity.
RESUMO
Antiferromagnet/ferromagnet (AFM/FM) bilayers that display the exchange bias (EB) effect have been subjected to intensive material research, being the key elements of novel spintronics systems. In a commonly accepted picture, the antiferromagnet, considered as a rigid material due to its high anisotropy and magnetic hardness, controls the magnetic properties of the ferromagnet, such as a shift of the hysteresis loop or coercivity. We show that this AFM-FM master-slave hierarchy is not generally valid and that the influence of the ferromagnet on the magnetic anisotropy (MA) of the neighbouring antiferromagnet must be considered. Our computer simulation and experimental studies of EB in an epitaxial CoO/Fe(110) bilayer show that the ferromagnetic layer with strong uniaxial magnetic anisotropy determines the interfacial spin orientations of the neighbouring AFM layer and rotates its easy axis. This effect has a strong feedback on the EB effect experienced by the FM layer. Our results show new physics behind the EB effect, providing a route for grafting a desired anisotropy onto the AFM and for precise tailoring of EB in AFM/FM systems.
RESUMO
PURPOSE: To compare cardiac function assessed by intraoperative transesophageal echocardiography in patients undergoing cardiac revascularization with or without cardiopulmonary bypass. MATERIAL AND METHODS: Forty-one patients scheduled for elective, isolated cardiac revascularization (21 on-pump and 20 off-pump) were prospectively analyzed. Patients were matched for demographic (age and gender), anthropometric (BMI), clinical (co-morbidities, EuroScore) and laboratory variables (blood counts, renal function, left ventricular function). Transesophageal echocardiography was performed after induction of anesthesia, protamine sulfate administration, and chest closure. Left ventricular wall motion score index, end-diastolic area, fractional area change, right ventricular area change and end-diastolic area were assessed. Troponin I and C-reactive protein concentrations were measured. RESULTS: Regarding echocardiographic parameters of left and right ventricular function no significant differences between on-pump and off-pump groups at any point-of-time measurements were found. Troponin I and C-reactive protein were higher in on-pump as compared to off-pump group (p=0.001 and p=0.002; p=0.003 and p=0.001, respectively). CONCLUSIONS: In elective patients scheduled for cardiac revascularization there were no difference in cardiac performance assessed by intraoperative echocardiography regardless of surgical method used.
Assuntos
Ponte de Artéria Coronária sem Circulação Extracorpórea/métodos , Ponte de Artéria Coronária/métodos , Ecocardiografia Transesofagiana/métodos , Idoso , Antropometria , Proteína C-Reativa/metabolismo , Estudos de Casos e Controles , Ecocardiografia/métodos , Feminino , Ventrículos do Coração/fisiopatologia , Humanos , Rim/fisiologia , Masculino , Pessoa de Meia-Idade , Estudos Prospectivos , Troponina I/sangue , Função Ventricular EsquerdaRESUMO
We investigate the dynamical properties of the non-heme iron (NHFe) in His-tagged photosynthetic bacterial reaction centers (RCs) isolated from Rhodobacter (Rb.) sphaeroides. Mössbauer spectroscopy and nuclear inelastic scattering of synchrotron radiation (NIS) were applied to monitor the arrangement and flexibility of the NHFe binding site. In His-tagged RCs, NHFe was stabilized only in a high spin ferrous state. Its hyperfine parameters (IS=1.06±0.01mm/s and QS=2.12±0.01mm/s), and Debye temperature (θ(D0)~167K) are comparable to those detected for the high spin state of NHFe in non-His-tagged RCs. For the first time, pure vibrational modes characteristic of NHFe in a high spin ferrous state are revealed. The vibrational density of states (DOS) shows some maxima between 22 and 33meV, 33 and 42meV, and 53 and 60meV and a very sharp one at 44.5meV. In addition, we observe a large contribution of vibrational modes at low energies. This iron atom is directly connected to the protein matrix via all its ligands, and it is therefore extremely sensitive to the collective motions of the RC protein core. A comparison of the DOS spectra of His-tagged and non-His-tagged RCs from Rb. sphaeroides shows that in the latter case the spectrum was overlapped by the vibrations of the heme iron of residual cytochrome c(2), and a low spin state of NHFe in addition to its high spin one. This enabled us to pin-point vibrations characteristic for the low spin state of NHFe.
Assuntos
Ferro/química , Complexo de Proteínas do Centro de Reação Fotossintética/química , Rhodobacter sphaeroides/química , Sítios de Ligação , Transporte de Elétrons , Ferro/metabolismo , Cinética , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Rhodobacter sphaeroides/crescimento & desenvolvimento , Rhodobacter sphaeroides/metabolismo , Espectroscopia de Mossbauer , Síncrotrons , VibraçãoRESUMO
An in-plane spin-reorientation transition occurring during the growth of epitaxial Fe films on W(110) was studied in situ by using the nuclear resonant scattering of synchrotron radiation. The spin-reorientation transition originates at the Fe/W(110) interface and proceeds via a noncollinear spin structure resembling a planar domain wall that propagates towards the surface with increasing film thickness.
RESUMO
Non-heme iron is a conservative component of type II photosynthetic reaction centers of unknown function. We found that in the reaction center from Rba. sphaeroides it exists in two forms, high and low spin ferrous states, whereas in Rsp. rubrum mostly in a low spin state, in line with our earlier finding of its low spin state in the algal photosystem II reaction center (Burda et al., 2003). The temperature dependence of the non-heme iron displacement studied by Mössbauer spectroscopy shows that the surrounding of the high spin iron is more flexible (Debye temperature ~165K) than that of the low spin atom (~207K). Nuclear inelastic scattering measurements of the collective motions in the Rba. sphaeroides reaction center show that the density of vibrational states, originating from non-heme iron, has well-separated modes between lower (4-17meV) and higher (17-25meV) energies while in the one from Rsp. rubrum its distribution is more uniform with only little contribution of low energy (~6meV) vibrations. It is the first experimental evidence that the fluctuations of the protein matrix in type II reaction center are correlated to the spin state of non-heme iron. We propose a simple mechanism in which the spin state of non-heme iron directly determines the strength of coupling between the two quinone acceptors (Q(A) and Q(B)) and fast collective motions of protein matrix that play a crucial role in activation and regulation of the electron and proton transfer between these two quinones. We suggest that hydrogen bond network on the acceptor side of reaction center is responsible for stabilization of non-heme iron in different spin states.
Assuntos
Bactérias/química , Proteínas de Bactérias/química , Ferro/química , Complexo de Proteínas do Centro de Reação Fotossintética/química , Bactérias/metabolismo , Proteínas de Bactérias/metabolismo , Transporte de Elétrons , Ferro/metabolismo , Cinética , Modelos Químicos , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Prótons , Quinonas/química , Quinonas/metabolismo , Rhodobacter sphaeroides/química , Rhodobacter sphaeroides/metabolismo , Rhodospirillum rubrum/química , Rhodospirillum rubrum/metabolismo , Espectroscopia de Mossbauer , Temperatura , VibraçãoRESUMO
We have engineered the magnetic properties of 1-8 nm Co films epitaxially grown on an Au-buffered bifacial W(110)/W(540) single crystal. The surface of Au/W(110) was atomically flat, whereas the Au/W(540) followed the morphology of the vicinal W surface, showing a regular array of monoatomic steps. For Co grown on Au/W(540), the existence of the out-of-plane magnetization component extended strongly to a thickness d of about 8 nm, which was accompanied by an anomalous increase of the out-of-plane switching field with increasing d. In addition, the process of up-down magnetization switching could be realized with both a perpendicular and in-plane external magnetic field.