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Chromium(VI) reductase activity is associated with the cytoplasmic membrane of anaerobically grown Shewanella putrefaciens MR‐1
- C. Myers, B. Carstens, W. Antholine, J. M. Myers
- Chemistry, MedicineJournal of applied microbiology
- 1 January 2000
Formate‐dependent Cr(VI) reductase activity was detected in anaerobically grown cells of S. putrefaciens MR‐1, with highest specific activity in the cytoplasmic membrane, suggesting involvement of a multi‐component electron transport chain which could include cytochromes and quinones.
The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus Bath
- D. Choi, Ryan C. Kunz, +7 authors A. DiSpirito
- Biology, MedicineJournal of bacteriology
- 1 October 2003
It is demonstrated that copper not only regulates the metabolic switch between the two methane monooxygenases but also regulates the level of expression of the pMMO and the development of internal membranes.
A novel eukaryotic factor for cytosolic Fe–S cluster assembly
- A. Roy, N. Solodovnikova, Tracy F Nicholson, W. Antholine, W. Walden
- Biology, MedicineThe EMBO journal
- 15 September 2003
A genetic screen to isolate Saccharomyces cerevisiae strains bearing mutations in genes required for the conversion of IRP1 to c‐aconitase led to the identification of a previously uncharacterized, essential gene, which is called CFD1 (cytosolic Fe–S cluster deficient).CFD1 encodes a highly conserved, putative P‐loop ATPase.
Chelation of intracellular iron with the antifungal agent ciclopirox olamine induces cell death in leukemia and myeloma cells.
Oral CPX prevented the engraftment of primary AML cells in nonobese diabetic/severe combined immunodeficiency mouse models, thereby establishing its ability to target leukemia stem cells and has previously unrecognized anticancer activity at concentrations that are pharmacologically achievable.
Spectral, kinetic, and thermodynamic properties of Cu(I) and Cu(II) binding by methanobactin from Methylosinus trichosporium OB3b.
To examine the potential role of methanobactin (mb) as the extracellular component of a copper acquisition system in Methylosinus trichosporium OB3b, the metal binding properties of mb were examined and suggested copper coordination changes at different Cu(II):mb ratios.
Assembly of Cytochrome-c Oxidase in the Absence of Assembly Protein Surf1p Leads to Loss of the Active Site Heme*
- Daniel Smith, J. Gray, L. Mitchell, W. Antholine, J. Hosler
- Biology, MedicineJournal of Biological Chemistry
- 6 May 2005
The data indicate that Surf1p plays a role in facilitating the insertion of heme a3 into the active site of cytochrome-c oxidase, and suggests that maturation of the heME a3-CuB center is a step that limits the association of subunits I and II in the assembly of mitochondrial cyto chrome oxidase.
Molecular features of the copper binding sites in the octarepeat domain of the prion protein.
The structure reveals an unusual complementary interaction between copper-structured HGGGW units that may facilitate molecular recognition between prion proteins, thereby suggesting a mechanism for transmembrane signaling and perhaps conversion to the pathogenic form.
Spectral and thermodynamic properties of Ag(I), Au(III), Cd(II), Co(II), Fe(III), Hg(II), Mn(II), Ni(II), Pb(II), U(IV), and Zn(II) binding by methanobactin from Methylosinus trichosporium OB3b.
- D. Choi, Young S Do, +15 authors A. DiSpirito
- Chemistry, MedicineJournal of inorganic biochemistry
- 1 December 2006
The binding of different metals by mb suggests that methanotrophic activity also may play a role in either the solubilization or immobilization of many metals in situ.
Copper coordination in the full-length, recombinant prion protein.
Rec recombinant, full-length Syrian hamster PrP is investigated using EPR methodologies and quantification studies reveal a fifth binding site in the flexible region between the octarepeats and the PrP globular C-terminal domain, which seems to provide a complete profile of the copper binding sites in PrP.
Vanadium(V) Reduction by Shewanella oneidensis MR-1 Requires Menaquinone and Cytochromes from the Cytoplasmic and Outer Membranes
- J. M. Myers, W. Antholine, C. Myers
- Medicine, BiologyApplied and Environmental Microbiology
- 1 March 2004
This is the first report delineating specific electron transport components that are required for V(V) reduction and of a role for OM cytochromes in the reduction of a soluble metal species.