Abstract
Fe(CN)6(-3) oxidation of the aerobically isolated 7Fe Azotobacter vinelandii ferredoxin I, (7Fe)FdI, is a degradative reaction. Destruction of the [4Fe-4S] cluster occurs first, followed by destruction of the [3Fe-3S] cluster. At a Fe(CN)6(-3)/(7Fe)FdI concentration ratio of 20, the product is a mixture of apoprotein and protein containing only a [3Fe-3S] cluster, (3Fe)FdI. This protein mixture, after partial purification, has been characterized by absorption, CD, magnetic CD, and EPR and Fe x-ray absorption spectroscopies. EPR and magnetic CD spectra provide strong evidence that the [3Fe-3S] cluster in (3Fe)FdI is essentially identical in structure to that in (7Fe)FdI. Analysis of the extended x-ray absorption fine structure (EXAFS) of (3Fe)FdI finds Fe scattering at an average Fe...Fe distance of approximately equal to 2.7 A. The structure of the oxidized [3Fe-3S] cluster in solutions of oxidized (3Fe)FdI, and, by extension, of oxidized (7Fe)FdI, is thus different from that obtained by x-ray crystallography on oxidized (7Fe)FdI. Possible interpretations of this result are discussed.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Adman E. T., Siefker L. C., Jensen L. H. Structure of Peptococcus aerogenes ferredoxin. Refinement at 2 A resolution. J Biol Chem. 1976 Jun 25;251(12):3801–3806. doi: 10.2210/pdb1fdx/pdb. [DOI] [PubMed] [Google Scholar]
- Antonio M. R., Averill B. A., Moura I., Moura J. J., Orme-Johnson W. H., Teo B. K., Xavier A. V. Core dimensions in the 3Fe cluster of Desulfovibrio gigas ferredoxin II by extended X-ray absorption fine structure spectroscopy. J Biol Chem. 1982 Jun 25;257(12):6646–6649. [PubMed] [Google Scholar]
- Beinert H., Emptage M. H., Dreyer J. L., Scott R. A., Hahn J. E., Hodgson K. O., Thomson A. J. Iron-sulfur stoichiometry and structure of iron-sulfur clusters in three-iron proteins: evidence for [3Fe-4S] clusters. Proc Natl Acad Sci U S A. 1983 Jan;80(2):393–396. doi: 10.1073/pnas.80.2.393. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burgess B. K., Jacobs D. B., Stiefel E. I. Large-scale purification of high activity Azotobacter vinelandII nitrogenase. Biochim Biophys Acta. 1980 Jul 10;614(1):196–209. doi: 10.1016/0005-2744(80)90180-1. [DOI] [PubMed] [Google Scholar]
- Emptage M. H., Kent T. A., Huynh B. H., Rawlings J., Orme-Johnson W. H., Münck E. On the nature of the iron-sulfur centers in a ferredoxin from Azotobacter vinelandii. Mössbauer studies and cluster displacement experiments. J Biol Chem. 1980 Mar 10;255(5):1793–1796. [PubMed] [Google Scholar]
- Freer S. T., Alden R. A., Carter C. W., Jr, Kraut J. Crystallographic structure refinement of Chromatium high potential iron protein at two Angstroms resolution. J Biol Chem. 1975 Jan 10;250(1):46–54. [PubMed] [Google Scholar]
- Ghosh D., Furey W., Jr, O'Donnell S., Stout C. D. Structure of a 7Fe ferredoxin from Azotobacter vinelandii. J Biol Chem. 1981 May 10;256(9):4185–4192. [PubMed] [Google Scholar]
- Ghosh D., O'Donnell S., Furey W., Jr, Robbins A. H., Stout C. D. Iron-sulfur clusters and protein structure of Azotobacter ferredoxin at 2.0 A resolution. J Mol Biol. 1982 Jun 15;158(1):73–109. doi: 10.1016/0022-2836(82)90451-x. [DOI] [PubMed] [Google Scholar]
- Huynh B. H., Moura J. J., Moura I., Kent T. A., LeGall J., Xavier A. V., Münck E. Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mössbauer and EPR studies. J Biol Chem. 1980 Apr 25;255(8):3242–3244. [PubMed] [Google Scholar]
- Kent T. A., Dreyer J. L., Kennedy M. C., Huynh B. H., Emptage M. H., Beinert H., Münck E. Mössbauer studies of beef heart aconitase: evidence for facile interconversions of iron-sulfur clusters. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1096–1100. doi: 10.1073/pnas.79.4.1096. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kent T. A., Huynh B. H., Münck E. Iron-sulfur proteins: spin-coupling model for three-iron clusters. Proc Natl Acad Sci U S A. 1980 Nov;77(11):6574–6576. doi: 10.1073/pnas.77.11.6574. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morgan T. V., Stephens P. J., Devlin F., Burgess B. K., Stout C. D. Selective oxidative destruction of iron-sulfur clusters. Ferricyanide oxidation of Azotobacter vinelandii ferredoxin I. FEBS Lett. 1985 Apr 22;183(2):206–210. doi: 10.1016/0014-5793(85)80777-8. [DOI] [PubMed] [Google Scholar]
- Morgan T. V., Stephens P. J., Devlin F., Stout C. D., Melis K. A., Burgess B. K. Spectroscopic studies of ferricyanide oxidation of Azotobacter vinelandii ferredoxin I. Proc Natl Acad Sci U S A. 1984 Apr;81(7):1931–1935. doi: 10.1073/pnas.81.7.1931. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Petering D., Fee J. A., Palmer G. The oxygen sensitivity of spinach ferredoxin and other iron-sulfur proteins. The formation of protein-bound sulfur-zero. J Biol Chem. 1971 Feb 10;246(3):643–653. [PubMed] [Google Scholar]
- Rydén L., Ofverstedt L. G., Beinert H., Emptage M. H., Kennedy M. C. Molecular weight of beef heart aconitase and stoichiometry of the components of its iron-sulfur cluster. J Biol Chem. 1984 Mar 10;259(5):3141–3144. [PubMed] [Google Scholar]
- Shulman R. G., Eisenberger P., Kincaid B. M. X-ray absorption spectroscopy of biological molecules. Annu Rev Biophys Bioeng. 1978;7:559–578. doi: 10.1146/annurev.bb.07.060178.003015. [DOI] [PubMed] [Google Scholar]
- Sweeney W. V. Proton magnetic resonance studies of Azotobacter vinelandii ferredoxin I. Evidence for a difference in coordination of the 3Fe centers in azotobacter vinelandii ferredoxin I and desulfovibrio gigas ferredoxin II. J Biol Chem. 1981 Dec 10;256(23):12222–12227. [PubMed] [Google Scholar]
- Sweeney W. V., Rabinowitz J. C., Yoch D. C. High and low reduction potential 4Fe-4S clusters in Azotobacter vinelandii (4Fe-4S) 2ferredoxin I. Influence of the polypeptide on the reduction potentials. J Biol Chem. 1975 Oct 10;250(19):7842–7847. [PubMed] [Google Scholar]
