Spectroscopic properties of desulfoferrodoxin from Desulfovibrio desulfuricans (ATCC 27774)
- PMID: 8144635
Spectroscopic properties of desulfoferrodoxin from Desulfovibrio desulfuricans (ATCC 27774)
Abstract
Desulfoferrodoxin, a non-heme iron protein, was purified previously from extracts of Desulfovibrio desulfuricans (ATCC 27774) (Moura, I., Tavares, P., Moura, J. J. G., Ravi, N., Huynh, B. H., Liu, M.-Y., and LeGall, J. (1990) J. Biol. Chem. 265, 21596-21602). The as-isolated protein displays a pink color (pink form) and contains two mononuclear iron sites in different oxidation states: a ferric site (center I) with a distorted tetrahedral sulfur coordination similar to that found in desulforedoxin from Desulfovibrio gigas and a ferrous site (center II) octahedrally coordinated with predominantly nitrogen/oxygen-containing ligands. A new form of desulfoferrodoxin which displays a gray color (gray form) has now been purified. Optical, electron paramagnetic resonance (EPR), and Mössbauer data of the gray desulfoferrodoxin indicate that both iron centers are in the high-spin ferric states. In addition to the EPR signals originating from center I at g = 7.7, 5.7, 4.1, and 1.8, the gray form of desulfoferrodoxin exhibits a signal at g = 4.3 and a shoulder at g = 9.6, indicating a high-spin ferric state with E/D approximately 1/3 for the oxidized center II. Redox titrations of the gray form of the protein monitored by optical spectroscopy indicate midpoint potentials of +4 +/- 10 and +240 +/- 10 mV for centers I and II, respectively. Mössbauer spectra of the gray form of the protein are consistent with the EPR finding that both centers are high-spin ferric and can be analyzed in terms of the EPR-determined spin Hamiltonian parameters. The Mössbauer parameters for both the ferric and ferrous forms of center II are indicative of a mononuclear high spin iron site with octahedral coordination and predominantly nitrogen/oxygen-containing ligands. Resonance Raman studies confirm the structural similarity of center I and the distorted tetrahedral FeS4 center in desulforedoxin and provide evidence for one or two cysteinyl-S ligands for center II. On the basis of the resonance Raman results, the 635 nm absorption band that is responsible for the gray color of the oxidized protein is assigned to a cysteinyl-S-->Fe(III) charge transfer transition localized on center II. The novel properties and possible function of center II are discussed in relation to those of mononuclear iron centers in other enzymes.
Similar articles
-
Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center.J Biol Chem. 1990 Dec 15;265(35):21596-602. J Biol Chem. 1990. PMID: 2174880
-
Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins.FEBS Lett. 1996 May 6;385(3):138-42. doi: 10.1016/0014-5793(96)00364-x. FEBS Lett. 1996. PMID: 8647238
-
A blue non-heme iron protein from Desulfovibrio gigas.Eur J Biochem. 1994 Dec 1;226(2):613-8. doi: 10.1111/j.1432-1033.1994.tb20087.x. Eur J Biochem. 1994. PMID: 8001576
-
Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies.Molecules. 2021 Aug 11;26(16):4852. doi: 10.3390/molecules26164852. Molecules. 2021. PMID: 34443440 Free PMC article. Review.
-
Insights into metalloproteins and metallodrugs from electron paramagnetic resonance spectroscopy.Curr Opin Chem Biol. 2021 Apr;61:114-122. doi: 10.1016/j.cbpa.2020.11.005. Epub 2021 Jan 7. Curr Opin Chem Biol. 2021. PMID: 33422836 Review.
Cited by
-
Probing the influence of local coordination environment on the properties of Fe-type nitrile hydratase model complexes.Inorg Chem. 2001 Mar 26;40(7):1646-53. doi: 10.1021/ic001271d. Inorg Chem. 2001. PMID: 11261975 Free PMC article.
-
Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase.Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3796-801. doi: 10.1073/pnas.0636858100. Epub 2003 Mar 24. Proc Natl Acad Sci U S A. 2003. PMID: 12655067 Free PMC article.
-
An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo.Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3802-7. doi: 10.1073/pnas.0537177100. Epub 2003 Mar 13. Proc Natl Acad Sci U S A. 2003. PMID: 12637682 Free PMC article.
-
The first crystal structure of class III superoxide reductase from Treponema pallidum.J Biol Inorg Chem. 2006 Jul;11(5):548-58. doi: 10.1007/s00775-006-0104-y. Epub 2006 May 6. J Biol Inorg Chem. 2006. PMID: 16791639
-
Discovery of superoxide reductase: an historical perspective.J Biol Inorg Chem. 2004 Mar;9(2):119-23. doi: 10.1007/s00775-003-0519-7. Epub 2004 Jan 13. J Biol Inorg Chem. 2004. PMID: 14722742 Review.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases