Magnetic Circular Dichroism of Low-Temperature-Grown AlxGa1-xAs

1995 ◽  
Vol 378 ◽  
Author(s):  
A. Prasad ◽  
X. Liu ◽  
P. Stallinga ◽  
E. R. Weber ◽  
A. K. Verma ◽  
...  

AbstractWe study magnetic circular dichroism of absorption (MCDA) of LT AlxGa1−xAs as a function of aluminum content. The MCDA spectrum of LT AlxGa1−xAs is distinctly different from the MCDA spectrum of LT GaAs, which has one paramagnetic and one diamagnetic peak at 0.95 eV and 1.18 eV, respectively. As the aluminum content increases, the spectrum of LT AlxGa1−xAs is dominated by a diamagnetic peak similar to the 1.18eV peak of the EL20-like defects in LT GaAs. However, the peak shifts to higher energies as x increases. The photoquenching and temperature dependence of this peak indicates an association with the EL2 defect. The paramagnetic peak observed in LT GaAs also shifts to higher energies but faster and eventually merges with the diamagnetic peak as the Al content increases. The study of the MCDA spectrum of LT AlxGa1−xAs as a function of aluminum content allows a better understanding of the MCDA phenomena of LT AlxGa1−xAs and LT GaAs, as well as the EL2-related transitions in bulk semi-insulating GaAs.

1976 ◽  
Vol 159 (3) ◽  
pp. 811-813 ◽  
Author(s):  
T Brittain ◽  
J Springall ◽  
C Greenwood ◽  
A J Thomson

The spin states of the haem components of mixed-valence cytochrome oxidase were studied at room temperature and at temperature down to 20K by using magnetic circular dichroism. The room-temperature studies show the presence of a low-spin ferrous haem together with a low-spin ferric haem, which we attribute to heams a3 and a respectively. At temperatures below 100K it appears that the CO of the mixed-valence CO complex may be irreversibly photolysed, and that in this case haems a and a3 assume their high-spin states. Thus in this enzyme haem-haem interactions appear possible at temperatures below 100K.


1981 ◽  
Vol 670 (1) ◽  
pp. 93-100 ◽  
Author(s):  
Andrew J. Thomson ◽  
A.Edward Robinson ◽  
Michael K. Johnson ◽  
Jose J.G. Moura ◽  
Isobel Moura ◽  
...  

1983 ◽  
Vol 215 (2) ◽  
pp. 303-316 ◽  
Author(s):  
C Greenwood ◽  
B C Hill ◽  
D Barber ◽  
D G Eglinton ◽  
A J Thomson

The visible-near-i.r.-region m.c.d. (magnetic-circular-dichroism) spectrum recorded at low temperature in the range 450-900 nm is reported for oxidized resting mammalian cytochrome c oxidase. M.c.d. magnetization curves determined at different wavelengths reveal the presence of two paramagnetic species. Curves at 576, 613 and 640 nm fit well to those expected for an x,y-polarized haem transition with g values of 3.03, 2.21 and 1.45, i.e. cytochrome a3+. The m.c.d. features at 515, 785 and 817 nm magnetize as a S = 1/2 paramagnet with average g values close to 2, and simulated m.c.d. magnetization curves obtained by using the observed g values of CuA2+, i.e. 2.18, 2.03 and 1.99, fit well to the experimental observations. The form of the m.c.d. magnetization curve at 466 nm is curious, but it can be explained if CuA2+ and cytochrome a3+ contribute with oppositely signed bands at this wavelength. By comparing the m.c.d. spectrum of the enzyme with that of extracted haem a-bisimidazole complex it has been possible to deconvolute the m.c.d. spectrum of CuA2+, which shows transitions throughout the spectral region from 450 to 950 nm. The m.c.d.-spectral properties of CuA2+ were compared with those of a well-defined type I blue copper centre in azurin isolated from Pseudomonas aeruginosa. The absolute intensities of the m.c.d. signals at equal fields and temperatures for CuA2+ are 10-20-fold greater than those for azurin. The optical spectrum of CuA2+ strongly suggests an assignment as a d9 ion rather than Cu(I) bound to a thiyl radical.


2002 ◽  
Vol 65 (24) ◽  
Author(s):  
R. Denecke ◽  
J. Morais ◽  
R. X. Ynzunza ◽  
G. H. Fecher ◽  
J. G. Menchero ◽  
...  

1997 ◽  
Author(s):  
R. Denecke ◽  
J. Morais ◽  
R. X. Ynzunza ◽  
J. G. Menchero ◽  
J. Liesegang ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document