Fourier transform studies of electron spin echo modulation of hemoglobin azide
- 1 August 1981
- journal article
- research article
- Published by AIP Publishing in The Journal of Chemical Physics
- Vol. 75 (3) , 1123-1125
- https://doi.org/10.1063/1.442158
Abstract
Electron spin echo modulation studies of hemoglobin have been carried out at 4.2 K at x band. Samples have been prepared from human blood. The modulation has been analyzed in the frequency domain by Fourier transforming the time domain data. The analysis indicates that the modulation arises from 14N of the histidine and of the porphyrin. The superhyperfine frequencies obtained from the Fourier transform results have been interpreted in terms of quadrupole coupling, dipolar and contact coupling with 14N.Keywords
This publication has 14 references indexed in Scilit:
- Analysis of the electron spin echo decay envelope for Nd3+:ATP complexesThe Journal of Chemical Physics, 1979
- The nuclear modulation effect in electron spin echoes for complexes of Cu2+ and imidazole with 14N and 15NThe Journal of Chemical Physics, 1978
- Nitrogen-14 nuclear quadrupole resonance spectra of coordinated imidazoleJournal of the American Chemical Society, 1978
- Electron spin echo envelope modulation of trapped radicals in disordered systems: nitrogen modulation from isotopically substituted chlorophyll a cationsChemical Physics Letters, 1978
- Structure and function of haemoglobinProgress in Biophysics and Molecular Biology, 1976
- Assignment of a ligand in stellacyanin by a pulsed electron paramagnetic resonance methodBiochemistry, 1976
- Nuclear quadrupole resonance of 14N in imidazole and related compoundsChemical Physics Letters, 1975
- Theory of E.P.R. in low-spin ferric haemoproteinsMolecular Physics, 1971
- An Analysis of the Electron Spin Resonance of Low Spin Ferric Heme CompoundsBiophysical Journal, 1970
- Binding in Hæmoglobin Azide as Determined by Electron Resonance: Electron Resonance Studies of Hæmoglobin Azide and Hydroxide DerivativesNature, 1957