"Ferredoxins" 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.
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
| Descriptor ID |
D005288
|
| MeSH Number(s) |
D12.776.097.350 D12.776.157.427.374.375.275 D12.776.556.579.374.375.275 D12.776.765.319
|
| Concept/Terms |
|
Below are MeSH descriptors whose meaning is more general than "Ferredoxins".
Below are MeSH descriptors whose meaning is more specific than "Ferredoxins".
This graph shows the total number of publications written about "Ferredoxins" by people in this website by year, and whether "Ferredoxins" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 1 | 0 | 1 |
| 1995 | 1 | 0 | 1 |
| 1996 | 1 | 0 | 1 |
| 1997 | 1 | 0 | 1 |
| 1999 | 1 | 0 | 1 |
| 2001 | 3 | 0 | 3 |
| 2002 | 1 | 0 | 1 |
| 2003 | 1 | 0 | 1 |
| 2004 | 2 | 0 | 2 |
| 2005 | 1 | 0 | 1 |
| 2006 | 2 | 0 | 2 |
| 2011 | 0 | 1 | 1 |
| 2013 | 0 | 1 | 1 |
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Below are the most recent publications written about "Ferredoxins" by people in Profiles.
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Ching TH, Yoza BA, Li QX. Quartet analysis of putative horizontal gene transfer in Crenarchaeota. J Mol Evol. 2014 Feb; 78(2):163-70.
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Tittabutr P, Cho IK, Li QX. Phn and Nag-like dioxygenases metabolize polycyclic aromatic hydrocarbons in Burkholderia sp. C3. Biodegradation. 2011 Nov; 22(6):1119-33.
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Mydel P, Takahashi Y, Yumoto H, Sztukowska M, Kubica M, Gibson FC, Kurtz DM, Travis J, Collins LV, Nguyen KA, Genco CA, Potempa J. Roles of the host oxidative immune response and bacterial antioxidant rubrerythrin during Porphyromonas gingivalis infection. PLoS Pathog. 2006 Jul; 2(7):e76.
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Kurtz DM. Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin. J Inorg Biochem. 2006 Apr; 100(4):679-93.
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Iyer RB, Silaghi-Dumitrescu R, Kurtz DM, Lanzilotta WN. High-resolution crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: facile, redox-dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins. J Biol Inorg Chem. 2005 Jun; 10(4):407-16.
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Jin S, Kurtz DM, Liu ZJ, Rose J, Wang BC. Displacement of iron by zinc at the diiron site of Desulfovibrio vulgaris rubrerythrin: X-ray crystal structure and anomalous scattering analysis. J Inorg Biochem. 2004 May; 98(5):786-96.
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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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Smoukov SK, Davydov RM, Doan PE, Sturgeon B, Kung IY, Hoffman BM, Kurtz DM. EPR and ENDOR evidence for a 1-His, hydroxo-bridged mixed-valent diiron site in Desulfovibrio vulgaris rubrerythrin. Biochemistry. 2003 May 27; 42(20):6201-8.
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Jin S, Kurtz DM, Liu ZJ, Rose J, Wang BC. X-ray crystal structures of reduced rubrerythrin and its azide adduct: a structure-based mechanism for a non-heme diiron peroxidase. J Am Chem Soc. 2002 Aug 21; 124(33):9845-55.
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Coulter ED, Kurtz DM. A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase. Arch Biochem Biophys. 2001 Oct 01; 394(1):76-86.