"Iron-Sulfur Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
| Descriptor ID |
D007506
|
| MeSH Number(s) |
D12.776.157.427.374.375 D12.776.556.579.374.375
|
| Concept/Terms |
Iron-Sulfur Proteins- Iron-Sulfur Proteins
- Proteins, Iron-Sulfur
- Iron Sulfur Proteins
- Proteins, Iron Sulfur
- Sulfur Proteins, Iron
|
Below are MeSH descriptors whose meaning is more general than "Iron-Sulfur Proteins".
Below are MeSH descriptors whose meaning is more specific than "Iron-Sulfur Proteins".
This graph shows the total number of publications written about "Iron-Sulfur Proteins" by people in this website by year, and whether "Iron-Sulfur Proteins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 1 | 0 | 1 |
| 1996 | 1 | 0 | 1 |
| 1998 | 2 | 0 | 2 |
| 2002 | 1 | 0 | 1 |
| 2003 | 1 | 1 | 2 |
| 2004 | 3 | 0 | 3 |
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Below are the most recent publications written about "Iron-Sulfur Proteins" by people in Profiles.
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Luckarift HR, Dalton H, Sharma ND, Boyd DR, Holt RA. Isolation and characterisation of bacterial strains containing enantioselective DMSO reductase activity: application to the kinetic resolution of racemic sulfoxides. Appl Microbiol Biotechnol. 2004 Nov; 65(6):678-85.
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Jin S, Kurtz DM, Liu ZJ, Rose J, Wang BC. X-ray crystal structure of Desulfovibrio vulgaris rubrerythrin with zinc substituted into the [Fe(SCys)4] site and alternative diiron site structures. Biochemistry. 2004 Mar 23; 43(11):3204-13.
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Bonomi F, Eidsness MK, Iametti S, Kurtz DM, Mazzini S, Morleo A. Contribution of the [FeII(SCys)4] site to the thermostability of rubredoxins. J Biol Inorg Chem. 2004 Apr; 9(3):297-306.
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Beharry ZM, Eby DM, Coulter ED, Viswanathan R, Neidle EL, Phillips RS, Kurtz DM. Histidine ligand protonation and redox potential in the rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase. Biochemistry. 2003 Nov 25; 42(46):13625-36.
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Emerson JP, Cabelli DE, Kurtz DM. 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 01; 100(7):3802-7.
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Cosper NJ, Eby DM, Kounosu A, Kurosawa N, Neidle EL, Kurtz DM, Iwasaki T, Scott RA. Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters. Protein Sci. 2002 Dec; 11(12):2969-73.
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Hanlon SP, Graham DL, Hogan PJ, Holt RA, Reeve CD, Shaw AL, McEwan AG. Asymmetric reduction of racemic sulfoxides by dimethyl sulfoxide reductases from Rhodobacter capsulatus, Escherichia coli and Proteus species. Microbiology (Reading). 1998 Aug; 144 ( Pt 8):2247-2253.
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Smith MA, Wehr K, Harris PL, Siedlak SL, Connor JR, Perry G. Abnormal localization of iron regulatory protein in Alzheimer's disease. Brain Res. 1998 Mar 30; 788(1-2):232-6.
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Garg RP, Vargo CJ, Cui X, Kurtz DM. A [2Fe-2S] protein encoded by an open reading frame upstream of the Escherichia coli bacterioferritin gene. Biochemistry. 1996 May 21; 35(20):6297-301.
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Dave BC, Czernuszewicz RS, Prickril BC, Kurtz DM. Resonance Raman spectroscopic evidence for the FeS4 and Fe-O-Fe sites in rubrerythrin from Desulfovibrio vulgaris. Biochemistry. 1994 Mar 29; 33(12):3572-6.