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85030944029
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The reader is referred to the introduction in Fritz et al. [2] for references to the early biochemical studies
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The reader is referred to the introduction in Fritz, et al. [2] for references to the early biochemical studies.
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2
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0015208458
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The iron electron nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida
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Fritz J., Anderson R.E., Fee J.A., Palmer G., Sands R.H., Tsibris J.C.M., Gunsalus I.C., Orme-Johnson W.H., Beinert H. The iron electron nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida. Biochim. Biophys. Acta. 253:1971;110-133.
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Hyde J.S., Maki A.H. ENDOR of a free radical in solution. J. Chem. Phys. 40:1964;3117-3118.
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Hyde J.S. ENDOR of free radicals in solution. J. Chem. Phys. 43:1965;1806-1818.
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and earlier publications referenced therein
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Rist G.H., Hyde J.S. Ligand ENDOR of metal complexes in powders. J. Chem. Phys. 52:1970;4633-4643. and earlier publications referenced therein.
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The number of iron atoms in the paramagnetic center (g=1.94) of reduced putidaredoxin, a non heme iron protein
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Tsibris J.C.M., Tsai R.C., Gunsalus I.C., Orme-Johnson W.H., Hansen R.E., Beinert H. The number of iron atoms in the paramagnetic center. (g=1.94) of reduced putidaredoxin, a non heme iron protein Proc. Natl. Acad. Sci. USA. 59:1968;959-965.
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0015208476
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The 2-iron ferredoxins in spinach, parsley, pig adrenal cortex, Azotobachter vinelandii and Clostridium pasteurianum: Studies by magnetic field Mössbauer spectroscopy
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Dunham W.R., Bearden A., Salmeen I., Palmer G., Sands R.H., Orme-Johnson W.H., Beinert H. The 2-iron ferredoxins in spinach, parsley, pig adrenal cortex, Azotobachter vinelandii and Clostridium pasteurianum: studies by magnetic field Mössbauer spectroscopy. Biochim. Biophys. Acta. 253:1971;134-152.
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Palmer, G.4
Sands, R.H.5
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Beinert, H.7
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10
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0014669928
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The magnetic susceptibility of oxidized and reduced ferredoxin from spinach and parsley and the high potential protein from chromatium
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Moss T.H., Petering D., Palmer G. The magnetic susceptibility of oxidized and reduced ferredoxin from spinach and parsley and the high potential protein from chromatium. J. Biol. Chem. 244:1969;2275-2277.
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Properties of spinach ferredoxin in anaerobic urea solutions: A comparison with the native protein
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Petering D., Palmer G. Properties of spinach ferredoxin in anaerobic urea solutions: a comparison with the native protein. Arch. Biochem. 141:1970;456-464.
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The magnetic susceptibility of spinach ferredoxin from 77-250°K: A measurement of the antiferromagnetic coupling between the two iron atoms
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Palmer G., Dunham W.R., Fee J.A., Sands R.H., Iizuka T., Yonetani I. The magnetic susceptibility of spinach ferredoxin from 77-250.°K: a measurement of the antiferromagnetic coupling between the two iron atoms Biochim. Biophys. Acta. 245:1971;201-207.
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Tetrahedral iron in the active center of plant ferredoxin and beef adrenodoxin
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Eaton W., Palmer G., Fee J.A., Kimura T., Lovenberg W. Tetrahedral iron in the active center of plant ferredoxin and beef adrenodoxin. Proc. Natl. Acad. Sci. USA. 68:1971;3015-3020.
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Contact-shifted NMR of spinach ferredoxin additional resonances and partial assignments
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Salmeen I.T., Palmer G. Contact-shifted NMR of spinach ferredoxin additional resonances and partial assignments. Arch. Biochem. Biophys. 150:1972;767-773.
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Spectroscopic studies on two-iron ferredoxins
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Sands R.H., Dunham W.R. Spectroscopic studies on two-iron ferredoxins. Q. Rev. Biophys. 7:1975;443-504.
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0019739089
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X-ray analysis of a [2Fe-2S] ferredoxin from Spirulina platensis, main chain fold and location of side chains at 2.5 Å resolution
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See, for example, Fig. 12 in
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See, for example, Fig. 12 in Tsukahara T., Fukayama K., Nakamura M., Katsube Y., Tanake N., Kakudo M., Wado K., Hase T., Matsubara H. X-ray analysis of a [2Fe-2S] ferredoxin from Spirulina platensis, main chain fold and location of side chains at 2.5. Å resolution J. Biochem. 90:1981;1763-1773.
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Kakudo, M.6
Wado, K.7
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EPR signal intensity and powder shapes: A reexamination
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Aasa R., Vanngard T. EPR signal intensity and powder shapes: a reexamination. J. Magn. Reson. 19:1975;308-315.
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85030941490
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personal communication to W.R.D
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W. Blumberg, personal communication to W.R.D.
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Blumberg, W.1
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0020486176
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Analysis of strain-induced EPR-line shapes and anisotropic spin lattice relaxation in a 2Fe-2S ferredoxin
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Hagen W.R., Albracht S.P.J. Analysis of strain-induced EPR-line shapes and anisotropic spin lattice relaxation in a 2Fe-2S ferredoxin. Biochim. Biophys. Acta. 702:1982;61-71.
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Albracht, S.P.J.2
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0001396992
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Quantitative numerical analysis of g strain in the EPR of distributed systems and its importance for multicenter metalloproteins
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Hagen W.R., Hearshen D.O., Harding L.J., Dunham W.R. Quantitative numerical analysis of g strain in the EPR of distributed systems and its importance for multicenter metalloproteins. J. Magn. Reson. 61:1985;233-244.
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0008876318
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An analysis of g strain in the EPR of two [2Fe-2S] ferredoxins: Evidence for a protein rigidity model
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Hearshen D.O., Hagen W.R., Sands R.H., Grande H.J., Crespi H.L., Gunsalus I.C., Dunham W.R. An analysis of g strain in the EPR of two [2Fe-2S] ferredoxins: evidence for a protein rigidity model. J. Magn. Reson. 69:1986;440-459.
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85030951123
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This work is unpublished in collaboration with M.L. Ludwig, D. Gatti, D.P. Ballou, on single crystals of phthalate dioxygenase reductase
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This work is unpublished in collaboration with M.L. Ludwig, D. Gatti, D.P. Ballou, on single crystals of phthalate dioxygenase reductase.
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28
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0018793861
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Temperature-dependent X-ray diffraction as a probe of structural dynamics
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