Mössbauer and EPR study of nitrosyl hemoglobin

H. D. Pfannes*, G. Bemski, E. Wajnberg, H. Rocha, E. Bill, H. Winkler, A. X. Trautwein

*Corresponding author for this work
7 Citations (Scopus)


Nitrosyl hemoglobin was prepared by bubbling fresh57Fe-enriched rat hemoglobin with NO. S- and X-band EPR spectra at 77 K are typical for an S=1/2 system with an anisotropic g-tensor and exhibit hyperfine interactions of14N with the electronic spin. Mössbauer spectra at 4.2 and 100 K consist of a superposition of spectra from high- and low-spin Fe(III), deoxygenated hemoglobin and a component corresponding to S=1/2, g=2, hyperfine constants Axx/gnΒn=Ayy/gnΒn=-19.6 T, Azz/gnΒn=6.8 T, quadrupole splitting δEQ=1.5 mm s-1, isomer shift Is=0.42 mm s-1 and linewidth 0.4 mm s-1. The spin-lattice relaxation rate at 100 K is <2×106 s-1.

Original languageEnglish
JournalHyperfine Interactions
Issue number1
Pages (from-to)797-802
Number of pages6
Publication statusPublished - 01.12.1994


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