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Mössbauer and EPR study of nitrosyl hemoglobin (1994)

Pfannes, H. -D. ; Bemski, G. ; Wajnberg, E. ; [et al.]

Springer

Hyperfine interactions 91 (1994), S. 797-802

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ISSN: 1572-9540

Source: Springer Online Journal Archives 1860-2000

Topics: Physics

Notes: 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 anS=1/2 system with an anisotropicg-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 toS=1/2,g=2, hyperfine constantsA xx /g n Β n =A yy /g n Β n =−19.6 T,A zz /g n Β n =6.8 T, quadrupole splitting δE Q=1.5 mm s−1, isomer shiftI 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02064609

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