@article {ISI:000254173600010,
	title = {N-heterocyclic carbene complexes of Rh: reaction with dioxygen without oxidation.},
	journal = {J. Am. Chem. Soc.},
	volume = {130},
	number = {12},
	year = {2008},
	month = {mar},
	pages = {3724{\textendash}5},
	abstract = {The reaction of oxygen with rhodium complexes containing N-heterocyclic carbenes was found to give dioxygen complexes with rare square planar geometries and unusually short O-O bond lengths. Analysis of the bonding in these complexes by Rh L-edge X-ray absorption spectroscopy (XAS), Raman spectroscopy, and DFT calculations provides evidence for a bonding model in which singlet oxygen is bound to a Rh(I) d8 metal complex, rather than the more common Rh(III) d6 peroxo species with octahedral geometry and O-O bond lengths in the 1.4-1.5 A range.},
	keywords = {chemical, DFT, dioxygen complexes, Heterocyclic Compounds, Heterocyclic Compounds: chemistry, METHANE, Methane: analogs \& derivatives, Methane: chemistry, models, MOLECULAR, molecular structure, ORGANOMETALLIC COMPOUNDS, Organometallic Compounds: chemical synthesis, Organometallic Compounds: chemistry, OXYGEN, Oxygen: chemistry, rhodium, Rhodium: chemistry, SPECTROMETRY, X-Ray Emission, X-Ray Emission: methods, XAS},
	issn = {1520-5126},
	doi = {10.1021/ja7108213},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/18321109},
	author = {Praetorius, Jeremy M and Allen, Daryl P and Wang, Ruiyao and Webb, Jonathan D and Grein, Friedrich and Kennepohl, Pierre and Crudden, Cathleen M}
}
@article {338,
	title = {De Novo terpenoid biosynthesis by the dendronotid nudibranch Melibe leonina},
	journal = {Chemoecology},
	volume = {12},
	number = {4},
	year = {2002},
	note = {ISI Document Delivery No.: 635GATimes Cited: 6Cited Reference Count: 23},
	pages = {199-202},
	type = {Article},
	abstract = {Stable isotope feeding studies using [1,2-C-13(2)]-sodium acetate have demonstrated that 2,6-dimetbyl-5-heptenal (1), a putative defensive allomone, is made by the Dendronotid nudibranch Melibe leonina via de novo biosynthesis.},
	keywords = {biosynthesis, CADLINA-LUTEOMARGINATA, chemical, CHEMICAL DEFENSE, defense nudibranch, DORID-NUDIBRANCHS, ECOLOGY, ISOTOPE INCORPORATION EVIDENCE, OPISTHOBRANCH MOLLUSK, ORIGIN, terpenoid, TRIOPHAMINE},
	isbn = {0937-7409},
	url = {<Go to ISI>://000180389600006},
	author = {Barsby, T. and Linington, R. G. and Andersen, R. J.}
}
@article {5031,
	title = {Artificial nucleases},
	journal = {Chembiochem},
	volume = {2},
	number = {10},
	year = {2001},
	note = {ISI Document Delivery No.: 479NGTimes Cited: 54Cited Reference Count: 25},
	month = {Oct},
	pages = {735-740},
	type = {Article},
	abstract = {The oxidation of DNA and RNA provides a facile approach for investigating the interaction of nucleic acids wit proteins and oligonucleotides In this article, we have outlined our understanding of the mechanism of DNA scission by 1,10-phenanthroline-copper(I) in the presence of hydrogen peroxide. We also discuss results obtained by using 1,10-phenanthroline - oligonucleotide conjugates in probing the size of the transcriptionally active open complex. Finally, we outline an effective method for converting DNA-binding proteins into site-specific modification agents by using 1,10-phenanthroline-copper(I).},
	keywords = {1, 10-PHENANTHROLINE-COPPER ION, chemical, COLI RNA-POLYMERASE, COMPLEX, copper, DNA, DNA cleavage, DNA recognition, ESCHERICHIA-COLI, NUCLEASE, nucleic acids, OLIGONUCLEOTIDES, PROTEIN, SITE-SPECIFIC NUCLEASE, TRANSCRIPTION INITIATION},
	isbn = {1439-4227},
	url = {<Go to ISI>://000171410000003},
	author = {Chen, C. H. B. and Milne, L. and Landgraf, R. and Perrin,David M. and Sigman, D. S.}
}
@article {5083,
	title = {Unstable trivalent arsenic metabolites, monomethylarsonous acid and dimethylarsinous acid},
	journal = {Journal of Analytical Atomic Spectrometry},
	volume = {16},
	number = {12},
	year = {2001},
	note = {ISI Document Delivery No.: 498MYTimes Cited: 95Cited Reference Count: 52},
	pages = {1409-1413},
	type = {Article},
	abstract = {Two key arsenic metabolites, monomethylarsonous acid (MMA(III)) and dimethylarsinous acid (DMA(III)), have recently been detected in human urine. There is an increasing interest in the speciation of these metabolites in humans because of their demonstrated effects on cellular toxicity and DNA damage. However, there is no information on the oxidative stability of these arsenic species. It is not known whether and to what extent these trivalent metabolites are changed during sample handling and storage. The objective of this study was to demonstrate the oxidative conversion of these arsenic species during sample storage. We compared the effects of the storage temperature (25, 4, and -20 degreesC) and storage duration (up to 5 months) on the stability of MMA(III) and DMA(III) in de-ionized water and in human urine. We used HPLC with hydride generation atomic fluorescence detection for the speciation of arsenic. This method provided sub-mug L-1 to low-mug L-1 detection limits for each arsenic species. We found that the oxidation of MMA(III) and DMA(III) was matrix and temperature dependent. Low temperature conditions (4 and -20 degreesC) improved the stability of these arsenic species over the room temperature storage condition. MMA(III) in de-ionized water was relatively stable for almost 4 months, when stored at 4 or -20 degreesC with less than 10\% of MMA(III) oxidized to MMA(V). In contrast, most of MMA(III) ( 90\%) in urine was oxidized to MMA(V) over the 5 month period under the 4 or -20 degreesC storage condition. At 25 degreesC, MMA(III) in urine was completely oxidized to MMA(V) within a week. DMA(III) in deionized water was stable for only 2-3 days, being rapidly oxidized to DMA(V). DMA(III) in urine was completely oxidized to DMA(V) within a day at 4 or -20 degreesC. The conversion of DMA(III) to DMA(V) in urine at 25 degreesC was complete in 17 h. These results show that MMA(III) and DMA(III) are much less stable than other arsenic species, and their stability depends on sample matrix and temperature.},
	keywords = {ATOMIC FLUORESCENCE DETECTION, BLACKFOOT DISEASE, chemical, DRINKING-WATER, ENZYMATIC, GLUTATHIONE-REDUCTASE, HUMAN HEPATOCYTES, HUMAN URINE, LIQUID-CHROMATOGRAPHY, METHYLATION, RABBIT LIVER, SPECIATION},
	isbn = {0267-9477},
	url = {<Go to ISI>://000172516100011},
	author = {Gong, Z. L. and Lu, X. F. and Cullen, W. R. and Le, X. C.}
}
@article {3720,
	title = {Multiple pathways for denaturation of horse plasma gelsolin},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {74},
	number = {1},
	year = {1996},
	note = {ISI Document Delivery No.: UE605Times Cited: 1Cited Reference Count: 38},
	pages = {101-107},
	type = {Article},
	abstract = {Gelsolin purified from horse plasma carries a surface charge distribution that greatly influences how the protein unfolds, aggregates, or precipitates as a function of temperature or concentration of chemical denaturant. Modification of gelsolin with fluorescein isothiocyanate replaces positive charges on amine groups with bulky, negatively charged fluorescein moieties. This postpones thermally induced precipitation by about 10 degrees C [Koepf, E.K., and Burtnick, L.D. 1993. Eur. J. Biochem. 212: 713-718]. Interaction with cations such as Ca2+ or guanidinium(+) also alters the surface charge on gelsolin. This affects the structure of the protein in solution, modifies the pathway for unfolding, and moderates the onset of precipitation induced by chemical denaturants or heat. Denaturation of gelsolin is not interpretable in terms of a simple two-state cooperative mechanism. The pathway to a denatured state and intermediate structures present along the way depend upon the agent used to unfold the protein.},
	keywords = {ACTIN-BINDING-SITES, calcium, chemical, circular dichroism, denaturation, FLUORESCEIN ISOTHIOCYANATE, gelsolin, PROTEIN, thermal},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1996UE60500011},
	author = {Koepf, E. K. and Burtnick, L. D.}
}
