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Cited by 5Electron Spin Resonance StudiesMagnetism in coordination complexesHemoglobin structure and function

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Electron spin relaxation time of Fe(III) in high spin heme proteins

Lanir, Amos·1977·Biochimica et Biophysica Acta (BBA) - General Subjects
DOI 10.1016/0304-4165(77)90136-2
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Abstract

The electron spin relaxation time of high spin Fe(III), taus, was determined from the frequency dependence (5-100 MHz) of the longitudinal proton relaxation rates of water in solutions of catalase, metmyoglobin and acid ferricytochrome c. In all three high-spin heme proteins the relaxation rates incrased below 25 MHz, while no frequency dependence was observed above that frequency. The results are interpreted by assuming that taus, which modulates the dipolar interaction between the unpaired electrons of the iron and the water protons, is frequently independent. Its value was determined to be (6 +/- 1) - 10(-11) s.

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References 25 · Cited by 5

Research works printed but not linked: 26

  1. Villafranca, 1976, FEBS Lett., 62, 230, 10.1016/0014-5793(76)80059-2 · DOI
  2. Levanon, 1970, J. Chem. Phys., 53, 876, 10.1063/1.1674152 · DOI
  3. Poupko, 1974, Mol. Phys., 5, 1345, 10.1080/00268977400101141 · DOI
  4. Lanir, 1975, Biochemistry, 14, 242, 10.1021/bi00673a008 · DOI
  5. Lanir, 1976, Biochemistry, 15, 2590, 10.1021/bi00657a017 · DOI
  6. Deisseroth, 1967, Arch. Biochem. Biophys., 120, 671, 10.1016/0003-9861(67)90533-4 · DOI
  7. Ginsburg, 1970, J. Sci. Instrum., 3, 699, 10.1088/0022-3735/3/9/306 · DOI
  8. George, 1958, 44, 1013
  9. Lanir, 1975, Arch. Biochem. Biophys., 166, 439, 10.1016/0003-9861(75)90407-5 · DOI
  10. Goldammer, 1975, Eur. J. Biochem., 57, 291, 10.1111/j.1432-1033.1975.tb02300.x · DOI
  11. Wuthrich, 1970, Struct. Bonding, 8, 53, 10.1007/3-540-05257-7_2 · DOI
  12. Lanir, 1975, FEBS Lett., 55, 254, 10.1016/0014-5793(75)81004-0 · DOI
  13. Villafranca, 1974, J. Biol. Chem., 249, 3532, 10.1016/S0021-9258(19)42604-5 · DOI
  14. Gupta, 1975, J. Biol. Chem., 250, 246, 10.1016/S0021-9258(19)42007-3 · DOI
  15. Luz, 1964, J. Chem. Phys., 40, 2686, 10.1063/1.1725581 · DOI
  16. Vuc-Pavlovic, 1974, Biophys. Chem., 2, 359, 10.1016/0301-4622(74)80063-3 · DOI
  17. Solomon, 1955, Phys. Rev., 99, 559, 10.1103/PhysRev.99.559 · DOI
  18. Bloembergen, 1957, J. Chem. Phys., 27, 572, 10.1063/1.1743771 · DOI
  19. Rubenstein, 1971, Mol. Phys., 20, 67, 10.1080/00268977100100081 · DOI
  20. Bloembergen, 1961, J. Chem. Phys., 34, 842, 10.1063/1.1731684 · DOI
  21. La Mar, 1973, J. Am. Chem. Soc., 95, 6950, 10.1021/ja00802a014 · DOI
  22. Griffin, 1975, J. Biol. Chem., 250, 6445, 10.1016/S0021-9258(19)41084-3 · DOI
  23. Fabry, 1974, J. Biol. Chem., 249, 2915, 10.1016/S0021-9258(19)42718-X · DOI
  24. Lahajnar, 1976, Int. J. Peptide Prot. Res., 8, 317, 10.1111/j.1399-3011.1976.tb02509.x · DOI
  25. Koenig, 1969, J. Biol. Chem., 244, 6520, 10.1016/S0021-9258(18)63493-3 · DOI
  26. Harris, 1974, J. Biol. Chem., 249, 5261, 10.1016/S0021-9258(19)42357-0 · DOI

Metadata

Authors
Lanir, A.
Affiliations
Tel Aviv University (IL)
Corresponding author
Lanir, Amos
Venue
Biochimica et Biophysica Acta (BBA) - General Subjects
Publisher
Elsevier BV
Published
1977-03
Volume
497
Issue
1
Pages
29-34
ISSN
0304-4165 (ISSN-L)
DOI
10.1016/0304-4165(77)90136-2
OpenAlex
W2030844890
Cited by
5
References
25
FWCI
0.37
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Electron Spin Resonance Studies
  • Physical Sciences › Materials Science › Electronic, Optical and Magnetic Materials › Magnetism in coordination complexes
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Keywords
electron spin relaxation time, high-spin Fe(III), heme proteins, catalase, metmyoglobin, proton spin-lattice relaxation, dipole-dipole interaction, frequency dependence, unpaired electrons
MeSH terms
Animals, Catalase, Cattle, Cytochrome c Group, Electron Spin Resonance Spectroscopy, Ferric Compounds, Horses, Hydrogen-Ion Concentration, Iron, Liver, Myocardium, Myoglobin, Whales

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