Inorganic Microbial Sulfur Metabolism

Abstract

Sulfate Transport: H.Cypionka, Sulfate Transport. Dissimilatory Sulfate Reduction: A. Dehydrogenases: Hydrogenases from Sulfate-Reducing Bacteria: T.A. Hansen and C.M.H. Hensgens, NAD-Dependent Alcohol Dehydrogenase from Desulfovibrio gigas. T.A. Hansen, NAD(P)-Independent Lactate Dehydrogenase from Sulfate-Reducing Prokaryotes. J.J.G. Moura and B.A.S. Barata, Aldehyde Oxidoreductases and Other Molybdenum-Containing Enzymes. R. Cammack, V.M.F. Lopez, and E.C. Hatchikian, Nickel-Iron Hydrogenase. D.S. Patil, Nickel-Iron-Selenium Hydrogenase. L.L. Barton, The Pyruvic Acid Phosphoroclastic Reaction. B. Electron Carrier Proteins from Sulfate-Reducing Bacteria: T. Yagi, Monoheme Cytochromes. I.B. Coutinho and A.V. Xavier, Tetraheme Cytochromes. M. Bruschi, Cytochrome c3 (Mr 26,000) Isolated from Sulfate-Reducing Bacteria and Its Relationships to Other Polyhemic Cytochromes from Desulfovibrio. Y. Higuchi, T. Yagi, and G. Voordouw, Hexadecaheme Cytochrome c. J.J.G. Moura, A.L. Macedo, and P.N. Palma, Ferredoxins. J. Vervoort, D. Heering, S. Peelen, and W. van Berkel, Flavodoxins. L.C. Sieker, R.E. Stenkamp, and J.LeGall, Rubredoxin in the Crystalline State. I. Moura, P. Tavares, and N. Ravi, Characterization of Three Proteins Containing Multiple Iron Sites: Rubrerythrin, Desulfoferrodoxin and a Protein Containing a Six-Iron Cluster. C. Terminal Reductases of Sulfate-Reducing Bacteria: J. Lampreia, A.S. Pereira, and J.J.G. Moura, Adenylylsulfate Reductases from Sulfate-Reducing Bacteria. J.M. Akagi, H.L. Drake, J.-H. Kim, and D. Gevertz, Thiosulfate and Trithionate Reductases. D.V. DerVartanian, Desulforubidin: Dissimilatory, High-Spin Sulfite Reductase of Desulfomicrobium Species. E.C. Hatchikian, Desulfofuscidin: Dissimilatory, High-Spin Sulfite Reductase of Thermophilic, Sulfate-Reducing Bacteria. I. Moura and A.R. Lino, Low-Spin Sulfite Reductases. M.-C. Liu, C. Costa, and I. Moura, Hexaheme Nitrite-Reductase from Desulfovibrio desulfuricans (ATCC 27774). D. Molecular Biology: W.M.A.M. van Dongen, J.P.W.G Stokkermans, and W.A.M. van der Berg, Genetic Manipulation of Desulfovibrio. C. Dahl, N. Speich, and H.G. Traper, Enzymology and Molecular Biology of Sulfate Reduction in the Extremely Thermophilic Archeon Archaeoglobus fulgidus. Dissimilatory Sulfur Reduction: G.D. Fauque, Sulfur Reductase from Thiophilic Sulfate-Reducing Bacteria. G.D. Fauque, O. Klimmek, and A. Kriger, Sulfur Reductases from Spirilloid Mesophilic Sulfur-Reducing Eubacteria. Oxidation of Reduced Sulfur Compounds: J.W. Ingledew and D.H. Boxer, Purification of Rusticyanin, a Blue Copper Protein from Thiobacillus ferrooxidans. B.F. Taylor, Adenylylsulfate Reductases from Thiobacilli. C. Dahl and H.G. Traper, Enzymes of Dissimilatory Sulfide Oxidation in Phototrophic Sulfur Bacteria. H.G. Traper, Reverse Siroheme Sulfite Reductase from Thiobacillus denitrificans. T.E. Meyer, Purification and Properties of Cytochrome c-555 from Phototrophic Green Sulfur Bacteria. T.E. Meyer, Purification and Properties of High-Potential Iron-Sulfur Proteins. I. Suzuki, Sulfite: Cytochrome c Oxidoreductase of Thiobacilli. I. Suzuki, Sulfur-Oxidizing Enzymes. T. Yamanaka, Sulfide-Cytochrome c Reductase (Flavocytochrome c). Metabolism of Polythionates: D.P. Kelly and A.P. Wood, Synthesis and Determination of Thiosulfate and Polythionates. D.P. Kelly and A.P. Wood, Enzymes Involved in the Microbiological Oxidation of Thiosulfate and Polythionates. D.P. Kelly and A.P. Wood, Whole-Organism Methods for Inorganic Sulfur Oxidation by Chemolithotrophs and Photolithotrophs. Special Techniques: B.H. Huynh, Missbauer Spectroscopy in Study of Cytochrome cd1 from Thiobacillus denitrificans, Desulfoviridin, and Iron Hydrogenase. H. Santos, P. Fareleira, J. LeGall, and A.V. Xavier, In Vivo Nuclear Magnetic Resonance in Study of Physiology of Sulfate-Reducing Bacteria. J.E. Wampler, Computational Chemistry and Molecular Modeling of Electron-Transfer Proteins. J.M. Odom and R.C. Ebersole, Immunoassay of Sulfate-Reducing Bacteria in Environmental Samples. Author Index. Subject Index.