Abstract
The temperature dependence of the EPR spectrum of oxidized high-potential iron protein from Chromatium vinosum has been studied. From line width and intensity measurements it is possible to determine the position of the first excited unoccupied state, 160 +/- 10 cm-1 above the ground state orbital.
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Selected References
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- Averill B. A., Herskovitz T., Holm R. H., Ibers J. A. Synthetic analogs of the active sites of iron-sulfur proteins. II. Synthesis and structure of the tetra(mercapto-m 3 -sulfido-iron) clusters, (Fe 4 S 4 (SR) 4 ) 2- . J Am Chem Soc. 1973 May 30;95(11):3523–3534. doi: 10.1021/ja00792a013. [DOI] [PubMed] [Google Scholar]
- Carter C. W., Jr, Kraut J., Freer S. T., Alden R. A., Sieker L. C., Adman E., Jensen L. H. A comparison of Fe 4 S 4 clusters in high-potential iron protein and in ferredoxin. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3526–3529. doi: 10.1073/pnas.69.12.3526. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dutton P. L., Petty K. M., Bonner H. S., Morse S. D. Cytochrome c2 and reaction center of Rhodospeudomonas spheroides Ga. membranes. Extinction coefficients, content, half-reduction potentials, kinetics and electric field alterations. Biochim Biophys Acta. 1975 Jun 17;387(3):536–556. doi: 10.1016/0005-2728(75)90092-4. [DOI] [PubMed] [Google Scholar]
- Gayda J. P., Gibson J. F., Cammack R., Hall D. O., Mullinger R. Spin lattice relaxation and exchange interaction in a 2-iron, 2-sulphur protein. Biochim Biophys Acta. 1976 May 20;434(1):154–163. doi: 10.1016/0005-2795(76)90045-3. [DOI] [PubMed] [Google Scholar]
- Gibson J. F., Hall D. O., Thornley J. H., Whatley F. R. The iron complex in spinach ferredoxin. Proc Natl Acad Sci U S A. 1966 Sep;56(3):987–990. doi: 10.1073/pnas.56.3.987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jelinek W., Darnell J. E. Double-stranded regions in heterogeneous nuclear RNA from Hela cells. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2537–2541. doi: 10.1073/pnas.69.9.2537. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Moss T. H., Petering D., Palmer G. The magnetic susceptibility of oxidized and reduced ferredoxins from spinach and parsley and the high potential protein from Chromatium. J Biol Chem. 1969 May 10;244(9):2275–2277. [PubMed] [Google Scholar]
- Poe M., Phillips W. D., McDonald C. C., Lovenberg W. Proton magnetic resonance study of ferredoxin from Clostridium pasteurianum. Proc Natl Acad Sci U S A. 1970 Apr;65(4):797–804. doi: 10.1073/pnas.65.4.797. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sands R. H., Dunham W. R. Spectroscopic studies on two-iron ferredoxins. Q Rev Biophys. 1974 Nov;7(4):443–504. doi: 10.1017/s0033583500001517. [DOI] [PubMed] [Google Scholar]
- Scholes C. P., Isaacson R. A., Feher G. Determination of the zero-field splitting of Fe 3+ in heme proteins from the temperature dependence of the spin-lattice relaxation rate. Biochim Biophys Acta. 1971 Jul 20;244(1):206–210. doi: 10.1016/0304-4165(71)90138-3. [DOI] [PubMed] [Google Scholar]
- Thomson A. J. A model of the tetrahedral iron cluster in iron-sulphur proteins. Biochem Soc Trans. 1975;3(4):468–472. doi: 10.1042/bst0030468b. [DOI] [PubMed] [Google Scholar]
- Yang C. Y., Johnson K. H., Holm R. H., Norman J. G., Jr Letter: Theoretical model for the 4-Fe active sites in oxidized ferredoxin and reduced "high-potential" proteins. Electronic structure of the analogue [Fe4S4(SCH3)4]2-. J Am Chem Soc. 1975 Oct 29;97(22):6596–6598. doi: 10.1021/ja00855a062. [DOI] [PubMed] [Google Scholar]
