Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and iron sulfide (Fe4S4) prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit

Biochemistry ◽  
1982 ◽  
Vol 21 (15) ◽  
pp. 3538-3547 ◽  
Author(s):  
Peter A. Janick ◽  
Lewis M. Siegel
Keyword(s):  
Escherichia Coli ◽  
Electron Paramagnetic Resonance ◽  
Iron Sulfide ◽  
Sulfite Reductase ◽  
Paramagnetic Resonance ◽  
Spectroscopic Evidence ◽  
Electron Paramagnetic ◽  
Prosthetic Groups

Spectroscopic Evidence for the Formation of the Mercurous Ion in Irradiated Acetates

1971 ◽  
Vol 49 (17) ◽  
pp. 2868-2873 ◽  
Author(s):  
R. S. Eachus ◽  
F. G. Herring
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Optical Spectroscopy ◽  
Mercuric Acetate ◽  
Cadmium Acetate ◽  
Γ Irradiation ◽  
Paramagnetic Resonance ◽  
Spectroscopic Evidence ◽  
Acetate Trihydrate ◽  
Electron Paramagnetic ◽  
Mercurous Ion

The Hg(I) center has been produced by γ-irradiation both in Hg(II) doped cadmium acetate trihydrate and pure mercuric acetate. Both electron paramagnetic resonance and optical spectroscopy have been used to identify this species. The results indicate that the Hg(I) ion is produced in a covalent environment.

Interaction of selectively spin-labeled 70S ribosomes with tRNAPhe. An electron paramagnetic resonance study

1981 ◽  
Vol 59 (5) ◽  
pp. 311-314 ◽  
Author(s):  
Angel Rodriguez ◽  
Hermann Dugas
Keyword(s):  
Escherichia Coli ◽  
Electron Paramagnetic Resonance ◽  
Structural Change ◽  
Ribosomal Proteins ◽  
Electron Paramagnetic Resonance Study ◽  
Paramagnetic Resonance ◽  
Trna Molecule ◽  
Sh Groups ◽  
Ribosome Structure ◽  
Electron Paramagnetic

70S ribosomes from Escherichia coli, selectively spin labeled on the SH groups of proteins S18, S12, S21, S17, and L27, were used to study the formation of the tertiary complex ribosome–poly(U)–tRNAPhe. Most of these ribosomal proteins are located in the region of binding of tRNA. The electron paramagnetic resonance observable structural change suggests a loosening of the ribosome structure upon binding of the tRNA molecule.

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