Spin the light off: rapid internal conversion into a dark doublet state quenches the fluorescence of an RNA spin label

2017 ◽  
Vol 19 (38) ◽  
pp. 26255-26264 ◽  
Author(s):  
Henrik Gustmann ◽  
Daniel Lefrancois ◽  
Andreas J. Reuss ◽  
Dnyaneshwar B. Gophane ◽  
Markus Braun ◽  
...  
Keyword(s):  
Spin Label ◽  
Internal Conversion ◽  
Doublet State ◽  
Nitroxide Group

The fluorescence of the RNA spin label Çm is quenched via rapid internal conversion into a dark doublet state, which is localized on the nitroxide group of the FNRO˙ compound.

Determination of nitroxide spin label conformations via PELDOR and X-ray crystallography

2016 ◽  
Vol 18 (15) ◽  
pp. 10428-10437 ◽  
Author(s):  
D. Abdullin ◽  
G. Hagelueken ◽  
O. Schiemann
Keyword(s):  
Spin Label ◽  
Nitroxide Group ◽  
X Ray ◽  
X Ray Crystallography ◽  
Position And Orientation ◽  
Good Agreement

PELDOR is used to unravel the position and orientation of MTSSL in six singly-labelled azurin mutants. A comparison with X-ray structures of the mutants shows good agreement with respect to the position and orientation of the nitroxide group.

A Nitroxide Diuron Analog as a Probe for the Mode of Action of Herbicides

1984 ◽  
Vol 39 (5) ◽  
pp. 342-346 ◽  
Author(s):  
Yona Siderer ◽  
Nelly Lavintman ◽  
Chaim Gilon ◽  
Itzhak Ohad
Keyword(s):  
Photosystem Ii ◽  
Spin Label ◽  
Mode Of Action ◽  
Electron Flow ◽  
Trypsin Treatment ◽  
Nitroxide Group ◽  
Psii Activity

A new spin label nitroxide which is also a herbicide of the urea family has been synthesized. The nitroxide spin label derivative of diuron (ditempuron, DTPU) inhibits electron flow at the site of diuron inhibition of photosystem II (PSII) activity, and it is also reduced by electron flow from one of the first acceptors of PSII. The reduction of the nitroxide group of DTPU is inhibited by diuron or by trypsin treatment of the thylakoids but not by DNP-INT or DBMIB. It is suggested that DTPU binds specifically to and accepts electrons at the Qв site.

Autoradiography with Isotopes Emitting Internal Conversion Electrons and Auger Electrons

1964 ◽  
Vol 2 (4) ◽  
pp. 241-262 ◽  
Author(s):  
S. Forberg ◽  
E. Odeblad ◽  
R. Söremark ◽  
S. Ullberg
Keyword(s):  
Internal Conversion ◽  
Auger Electrons ◽  
Conversion Electrons ◽  
Internal Conversion Electrons

scholarly journals The internal conversion of gamma-rays.—Part II

1928 ◽  
Vol 121 (787) ◽  
pp. 447-456
Keyword(s):  
Magnetic Field ◽  
Quantum Mechanics ◽  
Wave Equation ◽  
Gamma Rays ◽  
Internal Conversion ◽  
Scalar Potential ◽  
X Ray ◽  
Electro Magnetic Field ◽  
Γ Rays ◽  
Electro Magnetic

In a previous paper the absorption of γ-rays in the K-X-ray levels of the atom in which they are emitted was calculated according to the Quantum Mechanics, supposing the γ-rays to be emitted from a doublet of moment f ( t ) at the centre of the atom. The non-relativity wave equation derived from the relativity wave equation for an electron of charge — ε moving in an electro-magnetic field of vector potential K and scalar potential V is h 2 ∇ 2 ϕ + 2μ ( ih ∂/∂ t + εV + ih ε/μ c (K. grad)) ϕ = 0. (1) Suppose, however, that K involves the space co-ordinates. Then, (K. grad) ϕ ≠ (grad . K) ϕ , and the expression (K . grad) ϕ is not Hermitic. Equation (1) cannot therefore be the correct non-relativity wave equation for a single electron in an electron agnetic field, and we must substitute h 2 ∇ 2 ϕ + 2μ ( ih ∂/∂ t + εV) ϕ + ih ε/ c ((K. grad) ϕ + (grad. K) ϕ ) = 0. (2)

Lattice effect in solid state internal conversion

2009 ◽  
Vol 79 (3) ◽  
Author(s):  
Péter Kálmán ◽  
Tamás Keszthelyi
Keyword(s):  
Solid State ◽  
Internal Conversion ◽  
Lattice Effect

scholarly journals A spin label study of the thyroid hormone-binding sites in human plasma thyroxine transport proteins.

1981 ◽  
Vol 256 (2) ◽  
pp. 831-836
Author(s):  
S.Y. Cheng ◽  
G. Rakhit ◽  
F. Erard ◽  
J. Robbins ◽  
C.F. Chignell
Keyword(s):  
Thyroid Hormone ◽  
Human Plasma ◽  
Spin Label ◽  
Binding Sites ◽  
Transport Proteins ◽  
Hormone Binding ◽  
Label Study
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