Protein-tyrosyl radical interactions in photosystem II studied by electron spin resonance and electron nuclear double resonance spectroscopy: comparison with ribonucleotide reductase and in vitro tyrosine

Biochemistry ◽  
1992 ◽  
Vol 31 (47) ◽  
pp. 11874-11880 ◽  
Author(s):  
Curtis W. Hoganson ◽  
Gerald T. Babcock
Keyword(s):  
Electron Spin Resonance ◽  
Photosystem Ii ◽  
Ribonucleotide Reductase ◽  
Double Resonance ◽  
Resonance Spectroscopy ◽  
Tyrosyl Radical ◽  
Electron Nuclear Double Resonance ◽  
Spin Resonance ◽  
Double Resonance Spectroscopy

Electron Spin Resonance and Electron Nuclear Double Resonance Spectroscopy: Application to the Study of Trapped Electrons

1980 ◽  
Vol 34 (3) ◽  
pp. 293-295 ◽  
Author(s):  
Harold C. Box ◽  
Harold G. Freund
Keyword(s):  
Electron Spin Resonance ◽  
Electron Spin ◽  
Double Resonance ◽  
Resonance Spectroscopy ◽  
Electron Nuclear Double Resonance ◽  
Trapped Electrons ◽  
V Band ◽  
Endor Spectroscopy ◽  
Hydroxy Proton ◽  
Spin Resonance

V band electron spin resonance-ENDOR spectroscopy has been applied to the study of “trapped” electrons in single crystals of polyhydroxy and carbohydrate compounds X-irradiated at low temperature. Evidence is presented from ENDOR measurements of hydroxy proton couplings that electrons are stabilized at intermolecular sites. The electron can be stabilized in the dipole fields of two or three hydroxy groups.

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