Tobacco intervention training: current efforts and gaps in US medical schools.

Context: Research has documented that US medical schools inadequately teach tobacco intervention skills.

Objective: To examine effective training methods for tobacco intervention in undergraduate medical education.

Data Sources: Using indexing terms related to tobacco intervention and medical education, we searched MEDLINE (1966-June 2002) and the Cochrane Database of Systematic Reviews (through issue 2, 2002).

Facilities for chemical decontamination in accident and emergency departments in the United Kingdom.

Objective: To audit the facilities for chemical decontamination, with special reference to cyanide poisoning, in all major accident and emergency departments in the UK.

Method: A simple postal questionnaire was used to audit planning, premises, equipment, protection for staff, and stocks of specific antidotes to cyanide poisoning.

Results: 227 questionnaires from 261 departments (87%) were returned and used in the survey.

Removal of a cysteine ligand from rubredoxin: assembly of Fe(2)S(2) and Fe(S-Cys)(3)(OH) centres.

The electron transfer protein rubredoxin from Clostridium pasteurianum contains an Fe(S-Cys)(4) active site. Mutant proteins C9G, C9A, C42G and C42A, in which cysteine ligands are replaced by non-ligating Gly or Ala residues, have been expressed in Escherichia coli. The C42A protein expresses with a Fe(III)(2)S(2) cluster in place.

Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein.

Cox11 is a protein essential for respiratory growth and has been implicated in the assembly of the Cu(B) site of cytochrome c oxidase. In the present study, we demonstrate that Cox11 is a copper-binding protein. The soluble C-terminal domain of Cox11 forms a dimer that coordinates one Cu(I) per monomer via three thiolate ligands.

Structures of the cuprous-thiolate clusters of the Mac1 and Ace1 transcriptional activators.

X-ray absorption spectroscopy on the minimal copper-regulatory domains of the two copper-regulated transcription factors (Ace1 and Mac1) in Saccharomyces cerevisiae revealed the presence of a remarkably similar polycopper cluster in both proteins. The Cu-regulatory switch motif of Mac1 consisting of the C-terminal first Cys-rich motif, designated the C1 domain, binds four Cu(I) ions as does the Cu-regulatory domain of Ace1. The four Cu(I) ions are bound to each molecule in trigonal geometry.

Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions.

Extracellular copper regulates the DNA binding activity of the CopY repressor of Enterococcus hirae and thereby controls expression of the copper homeostatic genes encoded by the cop operon. CopY has a CxCxxxxCxC metal binding motif. CopZ, a copper chaperone belonging to a family of metallochaperones characterized by a MxCxxC metal binding motif, transfers copper to CopY.

Unraveling the substrate-metal binding site of ferrochelatase: an X-ray absorption spectroscopic study.

Ferrochelatase (EC 4.99.1.

Fatal non-cardiogenic pulmonary oedema after intravenous non-ionic radiographic contrast.

Life-threatening reactions to radiographic contrast media are rare. We describe a case of fatal non-cardiogenic pulmonary oedema, after use of iopamidol, a widely used, low osmolar, non-ionic, radiographic contrast medium. A woman with a history of bladder tumour who had haematuria was referred for an intravenous urogram.

Solution structural studies of molybdate-nucleotide polyanions.

The complexation of molybdate with the nucleotides adenosine-5'-monophosphate (5'-AMP), adenosine-3'-monophosphate (3'-AMP) and guanosine-5'-monophosphate (5'-GMP) has been investigated by (1)H and (31)P NMR and Mo K-edge X-ray absorption near edge (XANES) and extended X-ray absorption fine structure (EXAFS) spectroscopy. Acidification of aqueous solutions containing molybdate and each of the nucleotides resulted in the formation of a single species characterized by (1)H resonances which are deshielded relative to those of free nucleotide. Analysis of the two-component systems indicated a Mo/nucleotide ratio of 2.

Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism.

The combination of UV/visible/NIR absorption, CD and variable-temperature magnetic circular dichroism (VTMCD), EPR, and X-ray absorption (XAS) spectroscopies has been used to investigate the electronic and structural properties of the oxidized and reduced forms of Pyrococcus furiosus superoxide reductase (SOR) as a function of pH and exogenous ligand binding. XAS shows that the mononuclear ferric center in the oxidized enzyme is very susceptible to photoreduction in the X-ray beam. This observation facilitates interpretation of ground- and excited-state electronic properties and the EXAFS results for the oxidized enzyme in terms of the published X-ray crystallographic data (Yeh, A.

Kangaroo Mother Care in very low birth weight infants.

Objective: This study was conducted (i) to study through a randomized control trial the effect of Kangaroo Mother Care (KMC) on breast feeding rates, weight gain and length of hospitalization of very low birth neonates and (ii) to assess the acceptability of Kangaroo Mother Care by nurses and mothers.

Methods: Babies whose birth weight was less than 1500 Grams were included in the study once they were stable. The effect of Kangaroo Mother Care on breast feeding rates, weight gain and length of hospitalization of very low birth weight neonates was studied through a randomized control trial in 28 neonates.

Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein.

Sco1 is a conserved essential protein, which has been implicated in the delivery of copper to cytochrome c oxidase, the last enzyme of the electron transport chain. In this study, we show for the first time that the purified C-terminal domain of yeast Sco1 binds one Cu(I)/monomer. X-ray absorption spectroscopy suggests that the Cu(I) is ligated via three ligands, and we show that two cysteines, present in a conserved motif CXXXC, and a conserved histidine are involved in Cu(I) ligation.

Synthesis, characterization, and electrochemistry of cis-oxothio- and cis-bis(thio)tungsten(VI) complexes of hydrotris(3,5-dimethylpyrazol-1-yl)borate.

The complexes TpWO2X react with sulfiding agents such as B2S3 or P4S10 to give the oxothio- and bis(thio)tungsten(VI) complexes TpWOSX (X = Cl(-)) and TpWS2X [X = Cl(-), S2PPh2(-); Tp = hydrotris(3,5-dimethylpyrazol-1-yl)borate]. The reaction of TpWS2Cl with (i) PPh3 in pyridine and (ii) dimethyl sulfoxide affords TpWOSCl in good overall yield. The chloro complexes undergo metathesis with alkali metal salts to yield species of the type TpWOSX and TpWS2X [X = OPh(-), SPh(-), SePh(-), (-)-mentholate].

Molybdenum sequestration in Brassica species. A role for anthocyanins?

To elucidate plant mechanisms involved in molybdenum (Mo) sequestration and tolerance, Brassica spp. seedlings were supplied with molybdate, and the effects on plant physiology, morphology, and biochemistry were analyzed. When supplied with (colorless) molybdate Indian mustard (Brassica juncea) seedlings accumulated water-soluble blue crystals in their peripheral cell layers.

In situ observation of the generation of isothiocyanates from sinigrin in horseradish and wasabi.

Sulfur K-edge X-ray absorption spectroscopy has been used to determine the chemical identity of the sulfur-containing species in horseradish (Armoracia lapthifolia) and wasabi (Wasabia japonica) in situ, before and after cell disruption. The major sulfur-containing species in the intact root is sinigrin (1-thio-beta-D-glucopyranose 1-N-(sulfoxy)-3-buteneimidate) and related congeners. Disrupting the cells by applying local pressure allowed the conversion of the sulfur moieties in sinigrin to isothiocyanates and sulfate in approximately equimolar amounts.

Analysis of sulfur biochemistry of sulfur bacteria using X-ray absorption spectroscopy.

Many sulfide-oxidizing organisms, including the photosynthetic sulfur bacteria, store sulfur in "sulfur globules" that are readily detected microscopically. The chemical form of sulfur in these globules is currently the focus of a debate, because they have been described as "liquid" by some observers, although no known allotrope of sulfur is liquid at physiological temperatures. In the present work we have used sulfur K-edge X-ray absorption spectroscopy to identify and quantify the chemical forms of sulfur in a variety of bacterial cells, including photosynthetic sulfur bacteria.

Deep desulfurization of extensively hydrodesulfurized middle distillate oil by Rhodococcus sp. strain ECRD-1.

Dibenzothiophene (DBT), and in particular substituted DBTs, are resistant to hydrodesulfurization (HDS) and can persist in fuels even after aggressive HDS treatment. Treatment by Rhodococcus sp. strain ECRD-1 of a middle distillate oil whose sulfur content was virtually all substituted DBTs produced extensive desulfurization and a sulfur level of 56 ppm.

The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex.

Cox17 is the candidate copper metallochaperone for delivery of copper ions to the mitochondrion for assembly of cytochrome c oxidase. Cox17 purified as a recombinant molecule lacking any purification tag binds three Cu(I) ions per monomer in a polycopper cluster as shown by X-ray absorption spectroscopy. The CuCox17 complex exists in a dimer/tetramer equilibrium with a 20 microM k(d).

Structural basis of the antagonism between inorganic mercury and selenium in mammals.

Mercuric chloride toxicity in mammals can be overcome by co-administration of sodium selenite. We report a study of the mutual detoxification product in rabbit plasma, and of a Hg-Se-S-containing species synthesized by addition of equimolar mercuric chloride and sodium selenite to aqueous, buffered glutathione. Chromatographic purification of this Hg-Se-S species and subsequent structural analysis by Se and Hg extended X-ray absorption fine structure (EXAFS) spectroscopy revealed the presence of four-coordinate Se and Hg entities separated by 2.

Fate of selenate and selenite metabolized by Rhodobacter sphaeroides.

Cultures of a purple nonsulfur bacterium, Rhodobacter sphaeroides, amended with approximately 1 or approximately 100 ppm selenate or selenite, were grown phototrophically to stationary phase. Analyses of culture headspace, separated cells, and filtered culture supernatant were carried out using gas chromatography, X-ray absorption spectroscopy, and inductively coupled plasma spectroscopy-mass spectrometry, respectively. While selenium-amended cultures showed much higher amounts of SeO(3)(2-) bioconversion than did analogous selenate experiments (94% uptake for SeO(3)(2-) as compared to 9.

The active site structure of Thalassiosira weissflogii carbonic anhydrase 1.

X-ray absorption spectroscopy at the Zn K-edge indicates that the active site of the marine diatom Thalassiosira weissflogii carbonic anhydrase is strikingly similar to that of mammalian alpha-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 A.

Quantitative, chemically specific imaging of selenium transformation in plants.

Quantitative, chemically specific images of biological systems would be invaluable in unraveling the bioinorganic chemistry of biological tissues. Here we report the spatial distribution and chemical forms of selenium in Astragalus bisulcatus (two-grooved poison or milk vetch), a plant capable of accumulating up to 0.65% of its shoot dry biomass as Se in its natural habitat.