Coal dust exposures in the longwall mines of New South Wales, Australia: a respiratory risk assessment

This paper presents an analysis of personal respirable coal dust measurements recorded by the Joint Coal Board in the underground longwall mines of New South Wales from 1985 to 1999. A description of the longwall mining process is given. In the study, 11 829 measurements from 33 mines were analysed and the results given for each occupation, for seven occupational groups, for individual de-identified mines and for each year of study. The mean respirable coal dust concentration for all jobs was 1.51 mg/m(3) (SD 1.08 mg/m(3)). Only 6.9% of the measurements exceeded the Australian exposure standard of 3 mg/m(3). Published exposure-response relationships were used to predict the prevalence of progressive massive fibrosis and the mean loss of FEV1, after a working lifetime (40 years) of exposure to the mean observed concentration of 1.5 mg/m(3). Prevalences of 1.3 and 2.9% were predicted, based on data from the UK and the USA, respectively. The mean loss of FEV1 was estimated to be 73.7 ml.

Perforated corneal hydrops treated with sulfur hexafluoride (SF6) gas and tissue adhesive

Purpose: To report a case of a perforated acute hydrops in a mentally retarded patient that was successfully managed with intracameral sulfur hexafluoride gas and cyanoacrylate tissue adhesive. Methods: Interventional case report. Results: A 14-year-old mentally retarded male patient with keratoconus presented with a perforated acute hydrops. A bandage contact lens was applied. However, following a large emesis 2 days later, the aqueous leak worsened with shallowing of the anterior chamber. Under general anesthesia, sulfur hexafluoride was injected to reform the anterior chamber and cyanoacrylate tissue adhesive was applied to the perforated site and covered by a bandage contact lens and temporary tarsorrhaphy. A follow-up examination at 1 month showed a formed anterior chamber with tissue adhesive in situ and no aqueous leak. Conclusions: The successful use of intracameral sulfur hexafluoride and tissue adhesive in the management of perforated acute hydrops may avoid emergency tectonic penetrating keratoplasty and reduce potential complications in the poorly cooperative patient.

Sulfite : Cytochrome c oxidoreductase from Thiobacillus novellus - Purification, characterization, and molecular biology of a heterodimeric member of the sulfite oxidase family

Direct oxidation of sulfite to sulfate occurs in various photo- and chemotrophic sulfur oxidizing microorganisms as the final step in the oxidation of reduced sulfur compounds and is catalyzed by sulfite:cytochrome c oxidoreductase (EC 1.8.2.1), Here we show that the enzyme from Thiobacillus novellus is a periplasmically located alpha beta heterodimer, consisting of a 40.6-kDa subunit containing a molybdenum cofactor and an 8.8-kDa monoheme cytochrome c(552) smbunit (midpoint redox potential, Em(8.0) = +280 mV), The organic component of the molybdenum cofactor was identified as molybdopterin contained in a 1:1 ratio to the Mo content of the enzyme. Electron paramagnetic resonance spectroscopy revealed the presence of a sulfite-inducible Mo(V) signal characteristic of sulfite:acceptor oxidoreductases. However, pH-dependent changes in the electron paramagnetic resonance signal were not detected. Kinetic studies showed that the enzyme exhibits a ping-pong mechanism involving two reactive sites. K-m values for sulfite and cytochrome c(550) were determined to be 27 and 4 mu M, respectively; the enzyme was found to be reversibly inhibited by sulfate and various buffer ions. The sorAB genes, which encode the enzyme, appear to form an operon, which is preceded by a putative extracytoplasmic function-type promoter and contains a hairpin loop termination structure downstream of sorB. While SorA exhibits significant similarities to known sequences of eukaryotic and bacterial sulfite:acceptor oxidoreductases, SorB does not appear to be closely related to any known c-type cytochromes.

Enzymology and molecular biology of prokaryotic sulfite oxidation

Despite its toxicity, sulfite plays a key role in oxidative sulfur metabolism and there are even some microorganisms which can use it as sole electron source. Sulfite is the main intermediate in the oxidation of sulfur compounds to sulfate, the major product of most dissimilatory sulfur-oxidizing prokaryotes. Two pathways of sulfite oxidation are known: (1) direct oxidation to sulfate catalyzed by a sulfite: acceptor oxidoreductase, which is thought to be a molybdenum-containing enzyme; (2) indirect oxidation under the involvement of the enzymes adenylylsulfate (APS) reductase and ATP sulfurylase and/or adenylylsulfate phosphate adenylyltransferase with APS as an intermediate. The latter pathway allows substrate phosphorylation and occurs in the bacterial cytoplasm. Direct oxidation appears to have a wider distribution; however, a redundancy of pathways has been described for diverse photo- or chemotrophic, sulfite-oxidizing prokaryotes. In many pro- and also eukaryotes sulfite is formed as a degradative product from molecules containing sulfur as a heteroatom. In these organisms detoxification of sulfite is generally achieved by direct oxidation to sulfate. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

Simultaneous determination of delta(33) SV-CDT and delta S-34(V-CDT) using masses 48, 49 and 50 on a continuous flow isotope ratio mass spectrometer

A new, fast, continuous flow technique is described for the simultaneous determination of 633 S and delta(34)S using SO masses 48, 49 and 50. Analysis time is similar to5min/sample with measurement precision and accuracy better than +/-0.3parts per thousand. This technique, which has been set up using IAEA Ag2S standards S-1, S-2 and S-3, allows for the fast determination of mass-dependent or mass-independent fractionation (MIF) effects in sulfide, organic sulfur samples and possibly sulfate. Small sample sizes can be analysed directly, without chemical pre-treatment. Robustness of the technique for natural versus artificial standards was demonstrated by analysis of a Canon Diablo troilite, which gave a delta(33)S of 0.04parts per thousand and a delta(34)S of -0.06parts per thousand compared to the values obtained for S-1 of 0.07parts per thousand and -0.20parts per thousand, respectively. Two pyrite samples from a banded-iron formation from the 3710 Ma Isua Greenstone Belt were analysed using this technique and yielded MIF (Delta(33)S of 2.45 and 3.31parts per thousand) comparable to pyrite previously analysed by secondary ion probe. Copyright (C) 2004 John Wiley Sons, Ltd.

A recombinant diheme SoxAX cytochrome - Implications for the relationship between EPR signals and modified heme-ligands

The multiheme SoxAX proteins are notable for their unusual heme ligation (His/Cys-persulfide in the SoxA subunit) and the complexity of their EPR spectra. The diheme SoxAX protein from Starkeya novella has been expressed using Rhodobacter capsulatus as a host expression system. rSoxAX was correctly formed in the periplasm of the host and contained heme c in similar amounts as the native SoxAX. ESI-MS showed that the full length rSoxA, in spite of never having undergone catalytic turnover, existed in several forms, with the two major forms having masses of 28 687 +/- 4 and 28 718 +/- 4 Da. The latter form exceeds the expected mass of rSoxA by 31 4 Da, a mass close to that of a sulfur atom and indicating that a fraction of the recombinant protein contains a cysteine persulfide modification. EPR spectra of rSoxAX contained all four heme-dependent EPR signals (LS1a, LS1b, LS2, LS3) found in the native SoxAX proteins isolated from bacteria grown under sulfur chemolithotrophic conditions. Exposure of the recombinant SoxAX to different sulfur compounds lead to changes in the SoxA mass profile as determined by ESI while maintaining a fully oxidized SoxAX visible spectrum. Thiosulfate, the proposed SoxAX substrate, did not cause any mass changes while after exposure to dimethylsulfoxide a + 112 +/- 4 Da form of SoxA became dominant in the mass spectrum. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.