scholarly journals Multi-Cluster Allowed States and Spectroscopic Amplitude of Cluster Transfer

1977 ◽  
Vol 58 (1) ◽  
pp. 204-222 ◽  
Author(s):  
H. Horiuchi
Keyword(s):  
Cluster Transfer ◽  
Spectroscopic Amplitude

One-two step transfer observed in 16O+11B nuclear system

2015 ◽  
Vol 24 (06) ◽  
pp. 1550047 ◽  
Author(s):  
Sh. Hamada ◽  
N. Burtebayev
Keyword(s):  
Angular Distribution ◽  
Cross Section ◽  
Born Approximation ◽  
Optical Model ◽  
Ion Beam ◽  
Nuclear System ◽  
Distorted Wave ◽  
Distorted Wave Born Approximation ◽  
Cluster Transfer ◽  
Spectroscopic Amplitude

The angular distribution measurements for 16O ion beam elastically scattered from 11 B target of thickness 32.9μg/cm2 at energy 22.4 MeV had been performed in the cyclotron DC-60 INP NNC RK. The previous measurements for 16 O +11 B nuclear system at energies 27, 30, 32.5 and 35 MeV showed an increase in the differential cross-section at backward angles due to the contribution of cluster transfer. Such transfer process could not be described in terms of optical model (OM); it could be described within the framework of distorted wave Born approximation method implemented in FRESCO code. Both one (5 Li ) and two-step transfer (proton transfer followed by Alpha transfer) were taken into considerations. We have extracted the spectroscopic amplitude (SA) for the configuration 16 O →11 B +5 Li .

scholarly journals Role of α-Cluster Transfer in the Formation of 20Ne + 16O Cross-Sections at Backward Angles

2021 ◽  
Vol 51 (3) ◽  
pp. 780-787
Author(s):  
Sh. Hamada ◽  
Nourhan M. Elmedalaa ◽  
I. Bondouk ◽  
N. Darwish ◽  
Awad A. Ibraheem
Keyword(s):  
Cross Sections ◽  
Cluster Transfer

Analysing powers and differential cross sections of (3He,p) reactions on 6Li and 7Li at low energy

1995 ◽  
Vol 73 (1-2) ◽  
pp. 74-84 ◽  
Author(s):  
D. Baddou ◽  
C. Rioux ◽  
R. J. Slobodrian ◽  
J. M. Nelson
Keyword(s):  
Cross Sections ◽  
Differential Cross ◽  
Born Approximation ◽  
Low Energy ◽  
Angular Distributions ◽  
Differential Cross Sections ◽  
Distorted Wave ◽  
Distorted Wave Born Approximation ◽  
Nucleon Transfer ◽  
Cluster Transfer

Angular distributions of the differential cross sections and analysing powers were measured at an energy of 4.6 MeV. The results are compared with the distorted wave Born approximation predictions for two-nucleon transfer and for a deuteron-cluster transfer. The agreement is qualitative at best, and a discussion of alternatives to improve it is presented.

scholarly journals NADPH Inhibits [2Fe-2S] Cluster Protein Transfer from Diabetes Drug Target MitoNEET to an Apo-acceptor Protein

2012 ◽  
Vol 287 (15) ◽  
pp. 11649-11655 ◽  
Author(s):  
John A. Zuris ◽  
Syed S. Ali ◽  
Howard Yeh ◽  
Tung A. Nguyen ◽  
Rachel Nechushtai ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Oxidative Damage ◽  
Drug Target ◽  
Protein Transfer ◽  
Physiological Conditions ◽  
Founding Member ◽  
Cluster Transfer ◽  
Dependent Inhibition ◽  
Diabetes Drug ◽  
Transfer Properties

MitoNEET (mNT) is the founding member of the recently discovered CDGSH family of [2Fe-2S] proteins capable of [2Fe-2S] cluster transfer to apo-acceptor proteins. It is a target of the thiazolidinedione (TZD) class of anti-diabetes drugs whose binding modulate both electron transfer and cluster transfer properties. The [2Fe-2S] cluster in mNT is destabilized upon binding of NADPH, which leads to loss of the [2Fe-2S] cluster to the solution environment. Because mNT is capable of transferring [2Fe-2S] clusters to apo-acceptor proteins, we sought to determine whether NADPH binding also affects cluster transfer. We show that NADPH inhibits transfer of the [2Fe-2S] cluster to an apo-acceptor protein with an inhibition constant (Ki) of 200 μm, which reflects that of NADPH concentrations expected under physiological conditions. In addition, we determined that the strictly conserved cluster interacting residue Asp-84 in the CDGSH domain is necessary for the NADPH-dependent inhibition of [2Fe-2S] cluster transfer. The most critical cellular function of NADPH is in the maintenance of a pool of reducing equivalents, which is essential to counteract oxidative damage. Taken together, our findings suggest that NADPH can regulate both mNT [2Fe-2S] cluster levels in the cell as well as the ability of the protein to transfer [2Fe-2S] clusters to cytosolic or mitochondrial acceptors.

Cluster transfer reactions at low energies

1970 ◽  
Vol 29 (2-3) ◽  
pp. 143-158 ◽  
Author(s):  
M. El-Nadi ◽  
A. Osman ◽  
T. H. Rihan
Keyword(s):  
Transfer Reactions ◽  
Cluster Transfer ◽  
Low Energies

scholarly journals [2Fe-2S] cluster transfer in iron-sulfur protein biogenesis

2014 ◽  
Vol 111 (17) ◽  
pp. 6203-6208 ◽  
Author(s):  
L. Banci ◽  
D. Brancaccio ◽  
S. Ciofi-Baffoni ◽  
R. Del Conte ◽  
R. Gadepalli ◽  
...  
Keyword(s):  
Iron Sulfur ◽  
Cluster Transfer ◽  
Protein Biogenesis ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

scholarly journals Cytosolic iron-sulfur cluster transfer-a proposed kinetic pathway for reconstitution of glutaredoxin 3

FEBS Letters ◽  
2016 ◽  
Vol 590 (24) ◽  
pp. 4531-4540 ◽  
Author(s):  
Christine Wachnowsky ◽  
Insiya Fidai ◽  
James A. Cowan
Keyword(s):  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Cluster Transfer

Structure in multiplicity gated proton spectra in low energy 12C+93Nb reaction—compound nuclear process or massive cluster transfer?

2006 ◽  
Vol 765 (3-4) ◽  
pp. 277-293 ◽  
Author(s):  
A. Mitra ◽  
D.R. Chakrabarty ◽  
V.M. Datar ◽  
Suresh Kumar ◽  
E.T. Mirgule ◽  
...  
Keyword(s):  
Low Energy ◽  
Nuclear Process ◽  
Cluster Transfer ◽  
Massive Cluster ◽  
Reaction Compound
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