Mössbauer and EPR study of nitrosyl hemoglobin

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

doi:10.1007/BF02064609

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

Institute of Physics

7 Citations (Scopus)

Abstract

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 A_xx/g_nΒ_n=A_yy/g_nΒ_n=-19.6 T, A_zz/g_nΒ_n=6.8 T, quadrupole splitting δE_Q=1.5 mm s^-1, isomer shift I_s=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 language	English
Journal	Hyperfine Interactions
Volume	91
Issue number	1
Pages (from-to)	797-802
Number of pages	6
ISSN	0304-3834
DOIs	https://doi.org/10.1007/BF02064609
Publication status	Published - 01.12.1994

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title = "M{\"o}ssbauer and EPR study of nitrosyl hemoglobin",

abstract = "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. M{\"o}ssbauer 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.",

author = "Pfannes, {H. D.} and G. Bemski and E. Wajnberg and H. Rocha and E. Bill and H. Winkler and Trautwein, {A. X.}",

year = "1994",

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doi = "10.1007/BF02064609",

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volume = "91",

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T1 - Mössbauer and EPR study of nitrosyl hemoglobin

AU - Pfannes, H. D.

AU - Bemski, G.

AU - Wajnberg, E.

AU - Rocha, H.

AU - Bill, E.

AU - Winkler, H.

AU - Trautwein, A. X.

PY - 1994/12/1

Y1 - 1994/12/1

N2 - 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.

AB - 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.

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SP - 797

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JO - Hyperfine Interactions

JF - Hyperfine Interactions

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Mössbauer and EPR study of nitrosyl hemoglobin

Abstract

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