Spectroscopic studies on two-iron ferredoxins

Quarterly Reviews of Biophysics

Volumn 7, Issue 4, 1974, Pages 443-504

  Sands, R H ^a   Dunham, W R ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FERREDOXIN; IRON;

AZOTOBACTER; BACTERIUM; CLOSTRIDIUM; IN VITRO STUDY; MICROORGANISM; THEORETICAL STUDY;

ADRENAL CORTEX; ALGAE; AMINO ACID SEQUENCE; ANIMAL; AZOTOBACTER; CATTLE; CHLORELLA; CLOSTRIDIUM; ELECTRON SPIN RESONANCE SPECTROSCOPY; FERREDOXINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CONFORMATION; MOLECULAR WEIGHT; NUCLEAR PHYSICS; PLANTS; SPECTRUM ANALYSIS; SUPPORT, U.S. GOV'T, P.H.S.; SWINE;

EID: 0016249116     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583500001517     Document Type: Article

References (58)

1. Abragram, A.&Bleaney, A. (1970). EPR of Transition Ions. London, New York : Oxford University Press (Clarendon).
2. Aggarwal, S. T., Rao, K. K.&Matsubara, H. (1971). Horsetail ferredoxin: isolation and some chemical studies. J. Biochem. 69, 601.
3. Anderson, R. E. (1972). Study of the active sites of ferrodoxin from Synechococcus lividus. Thesis, University of Michigan, Ann Arbor, Michigan, U.S.A. Available from University Microfilms, 300 No. Zeeb Road, Ann Arbor, Michigan 48103 order no. 73–11032.
4. Anderson, R. E., Sands, R. H.&Crespi, H. (1974). In preparation.
5. Ayscough, P. B. (1967). Electron Spin Resonance in Chemistry. London: Methuen.
6. Beinert, H.&Orme-Johnson, W. H. (1960). Electron-nuclear and electron-electron spin interactions in the study of enzyme structure and function. Ann. N.Y. Acad. Sci. 158, 336.
7. Bersohn, M.&Baird, J. C. (1966). An Introduction to EPR. New York: Benjamin.
8. Brintzinger, H., Palmer, G.&Sands, R. C. (1966a). An electron paramagnetic resonance study of metal-aromatic bonding in Bis(hexamethylbenzene) iron (I). J. Am. Chem. Soc. 88, 623.
9. Brintzinger, H., Palmer, G.&Sands, R. C. (1966b). The ligand field or iron in ferredoxin from spinach chloroplasts and related non heme iron enzymes. Proc. natn. Acad. Sci. U.S.A. 55, 397.
10. Carrington, A.&McLachlan, A. C. (1967). Introduction to Magnetic Resonance. New York : Harper.
11. De Benedetti, S., De S. Barros, F.&Hoy, G. R. (1966). Chemical and structural effects on nuclear radiations. Am. Rev. Nucl. Sci. 16, 31.
12. Der Vartanian, D. V., Orme-Johnson, W. H., Hansen, R. E., Beinert, H., Tsai, R. L., Tsibris, J. C., Bartholomaus, R. C.&Gunsalus, I. C. (1967). Identification of sulfur as component of the EPR signal at g = 1–94 by isotopic substitution. Biochem. biophys. Res. Commun. 26,569.
13. Dunham, W. R. (1970). The active center of the plant-type ferredoxins: studies by Mossbauer spectroscopy. Thesis, University of California, La Jolla, California. University Microfilms no. 70–19.
14. Dunham, W. R., Bearden, A., Salmeen, I., Palmer, G., Sands R. H., Orme-Johnson, W. H.&Beinert, C. (1971a). The 2-iron ferredoxins in spinach, parsley, pig adrenal cortex, Azotobacter vinelandii and Clostridium pasteurianum : studies by Magnetic field Mossbauer spectroscopy. Biochim. biophys. Acta 253, 134.
15. Dunham, W. R., Palmer, G., Sands, R. H., Bearden, A. J., Beinert, H.&Orme-Johnson, W. H. (1971 b). Comments on‘The interpretation of the EPR and Mossbauer spectra of two-iron, one-electron iron-sulfur proteins’. Biochem. biophys. Res. Commun. 45, 1119.
16. Dunham, W. R., Palmer, G., Sands, R. H.&Bearden, A. J. (1971c). On the structure of the iron-sulphur complex in the 2-iron ferredoxins. Biochim. Biophys. Acta 253, 373.
17. Eaton, W. A., Palmer, G., Fee, J. A., Kimura, T.&Lovenberg, W. (1971). Tetrahedral iron in the active center of plant ferredoxins and beef adrenodoxin. Proc. natn. Acad. Set. U.S.A. 68, 3015.
18. Feher, G., Isaacson, R. A., Scholes, C. P.&Hazel, R. (1972). Electron nuclear double resonance (ENDOR) investigation on myoglobin and hemoglobin. Ann. N.Y. Acad. Sci. Proc. Fifth Int. Conf.: Magnetic Resonance in Biological Systems, New York, 4–8 December 1972.
19. Fritz, J., Anderson, R., Fee, J., Palmer, G., Sands, R. H., Orme-Johnson, W. H., Beinert, H., Tsibris, J. C. M.&Gunsalus, I. C. (1971). The iron electron-nuclear double resonance (endor) of 2-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida. Biochim. biophys. Acta 253, 110.
20. Fry, K. T., Lazarini, R. A.&San Pietro, A. (1963). The photoreduction of iron in photosynthetic pyridine nucleotide reductase. Proc. natn. Acad. Set. U.S.A. 50, 652.
21. Gersmann, H. R.&Swalen, J. D. (1962). Electron paramagnetic resonance spectra of copper complexes. J. Chem. Phys. 36, 3221.
22. Gibson, J. F., Hall, D. O., Thornley, J. H. M.&Whatley, F. R. (1966). The iron complex in spinach ferredoxin. Proc. natn. Acad. Sci. U.S.A. 56, 987.
23. Gruber, S. J., Harris, C. M.&Sinn, E. (1968). Metal complexes as ligands. VI. Antiferromagnetic interactions in trinuclear complexes containing similar and dissimilar metals. J. Chem. Phys. 49, 2183.
24. Hall, D. O.&Evans, M. C. W. (1969). Iron-sulphur proteins. Nature, Lond. 223, 1342.
25. Herskovitz, T., Averill, A. A., Holm, R. H., Ivers, J. A., Phillips, W. D.&Weiher, J. F. (1972). Structure and properties of a synthetic analogue of bacterial iron-sulphur proteins. Proc. natn. Acad. Set. U.S.A. 69, 2437.
26. Hudson, A. (1971). Nuclear hyperfine interactions in trimeric clusters. Molec. Phys. 21, 61.
27. Kneubuhl, F. K.&Natterer, A. (1961). Paramagnetic resonance intensity of anisotropic substances and its influence on line shapes. Helv. Phys. Acta 34, 710.
28. Lang, G. (1970). Mössbauer spectroscopy of haem proteins. Q. Rev. Biophys. 3. 1.
29. La Mar, G. N., Eaton, G. R., Holm, R. H.&Walker, F. A. (1973). Proton magnetic resonance investigation of antiferromagnetic oxy-bridged ferric dimers and related high-spin monomeric ferric complexes. J. Am. Chem. Soc. 95, 63.
30. Lippard, S. J. (1972). Iron-sulfur coordination compounds and proteins. Accts Chem. Res. 6, 282.
31. Lovenberg, W. (ed.) (1973). Iron-sulfur Proteins. New York, London: Academic Press.
32. Malley, I. I. (1965). Electron paramagnetic resonance lineshapes of randomly oriented fixed molecules. I. Axially symmetric g-tensor and hyperfine interactions. J. Molec. Spectrosc. 17, 210.
33. Mayerle, J. J., Frankel, R. B., Holm, R. C., Ibers, J. A., Phillips, W.&Weiher, J. F. (1973). Synthetic analogs of the active sites of iron-sulfur proteins. Structure and properties of Bis [o-xyldithiolate-u2-sulfidoferrate (III)]. An analog of the 2Fe-2S proteins. Proc. natn. Acad. Sci. U.S.A. 70, 2429.
34. Mayhew, S. G., Petering, D., Palmer, G.&Foust, G. (1969). Spectrophotometry titration of ferredoxins and chromatium high potential iron protein with sodium dithionite. J. biol. Chem. 244, 2830.
35. Moriya, T. (1960). Anisotropic super exchange interaction and weak ferromagnetism. Phys. Rev. 120, 91.
36. Moss, T. H., Petering, D.&Palmer, G. (1969). The magnetic susceptibility of oxidized and reduced ferredoxin from spinach and parsley and the high potential protein from chromatium. J. biol. Chem. 244, 2275.
37. Munck, E., Debrunner, P. G., Tsibris, J. C. M.&Gunsalus, I. C. (1972). Mossbauer parameters of putidaredoxin and its selenium analog. Biochemistry, N.Y. 11, 855.
38. Neiman, R.&Kivelson, D. (1961). ESR line shapes in glasses of copper complexes. J. Chem. Phys. 35, 156.
39. Newman, D. J., Ihle, J. N.&Dure, III, L. (1969). Chemical composition of a ferredoxin isolated from cotton. Biochem. biophys. Res. Commun. 36,947.
40. Orme-Johnson, W. H.&Beinert, H. (1969a). The magnetic susceptibility of oxidised and reduced ferredoxins from spinach and parsley and the high potential protein from chromatium. J. biol. Chem. 244, 6143.
41. Orme-Johnson, W. H.&Beinert, C. (1969 b). Heterogeneity of paramagnetic species in two iron-sulfur proteins: Clostridium pasteurianum ferredoxin and milk xanthine oxidase. Biochem. biophys. Res. Commun. 36, 337.
42. Orme-Johnson, W. H., Hansen, R. E., Beinert, H., Tsibris, J. C. M., BartholomAus, R. C.&Gunsalus, I. C. (1968). On the sulphur components of iron-sulphur proteins. 1. The number of acid-labile sulphur groups sharing an unpaired electron with iron. Proc. natn. Acad. Sci. U.S.A. 60, 368.
43. Owen, J. (1972). Chapter 6, sect. 5 in Electron Paramagnetic Resonance (ed. S. Geschwind). Plenum.
44. Palmer, G., Dunham, W. R., Fee, J. A., Sands, R. H., Iikuza, T.&Yonetani, I. (1971). 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, 201.
45. Palmer, G.&Sands, R. H. (1966). On the magnetic resonance of spinach ferredoxin. J. biol. Chem. 241, 253.
46. Peisach, J., Blumberg, W. E., Lode, E. T.&Coon, M. J. (1971). An analysis of the electron paramagnetic resonance spectrum of Pseudomonas oleovorans rubredixon. J. biol. Chem. 246, 5877.
47. Petering, D. H., Fee, J. A.&Palmer, G. (1971). The oxygen sensitivity of spinach ferredoxin and other iron sulphur proteins. J. biol. Chem. 246, 643.
48. Petering, D. H.&Palmer, G. (1970). Properties of spinach ferredoxin in anaerobic urea solutions: a comparison with the native protein. Archs Biochem. 141, 456.
49. Poe, M., Phillips, W. D., Glickson, J. D.&San Pietro, A. (1971). Proton magnetic resonance studies of the ferredoxins from spinach and parsley. Proc. natn. Acad. Set. U.S.A. 68, 68.
50. Salmeen, I. T. (1970). The interpretation of electron paramagnetic resonance and Mossbauer spectra of iron-sulfur proteins of the plant ferredoxin type. Thesis, University of Michigan, Ann Arbor, Michigan, U.S.A. Available from University Microfilms, 300 No, Zeeb Road, Ann Arbor, Michigan 48103, order No. 70–4181.
51. Salmeen, I. T.&Palmer, G. (1972). Contact-shifted NMR of spinach ferredoxin additional resonances and partial assignments. Archs Biochem. Biophys. 150, 767.
52. Shethna, Y. I., Wilson, P. W., Hansen, R. E.&Beinert, H. (1964). Identification by isotopic substitution of the EPR signal atg = 1.94 in a non-heme iron protein from Azotobacter. Proc. natn. Acad. Sci. U.S.A. 52, 1263.
53. Sieker, L. C., Adman, E.&Jensen, L. H. (1973). Structure of the Fe-S complex in a bacterial ferredoxin. Nature, Lond. 235, 40.
54. Singer, T. P.&Massey, V. (1957). Experimental foundations of the concept of metal-flavo protein catalysis. Rec. Chem. Prog. 18, 201.
55. Stahs, G.&Kraut, J. (1968). Low resolution electron-density and anomalous-scattering-density maps of chromatium high potential iron protein. J. molec. Biol. 35, 503.
56. Thornley, J. H. M., Gibson, J. F., Whatley, F. R.&Hall, D. O. (1966). Comment on a recent model of the iron complex in spinach ferredoxin. Biochem. biophys. Res. Commun. 24, 877.
57. Tsibris, J. C. M., Tsai, R. L., Gunsalus, I. C., Orne-Johnson, W. H., Hansen, R. E.&Beinert, H. (1968). The number of iron atoms in the paramagnetic center (g = 1–94) of reduced putideredoxin, a non heme iron protein. Proc. natn. Acad. Set. U.S.A. 59, 959.
58. Werts, J. E.&Bolton, J. R. (1972). Electron Spin Resonance, Elementary Theory and Practical Applications. New York: McGraw-Hill.