The Resource Inorganic microbial sulfur metabolism, edited by Harry D. Peck, Jr., Jean LeGall

Inorganic microbial sulfur metabolism, edited by Harry D. Peck, Jr., Jean LeGall

Label
Inorganic microbial sulfur metabolism
Title
Inorganic microbial sulfur metabolism
Statement of responsibility
edited by Harry D. Peck, Jr., Jean LeGall
Contributor
Subject
Genre
Language
eng
Member of
Cataloging source
NLM
Illustrations
illustrations
Index
index present
LC call number
QP601
LC item number
.M49 v.243
Literary form
non fiction
NAL call number
QP601.M49
NAL item number
v.243
Nature of contents
bibliography
NLM call number
  • W1
  • QD 181.S1
NLM item number
  • ME9615K v.243 1994
  • I58 1994
http://library.link/vocab/relatedWorkOrContributorName
  • Peck, Harry D
  • LeGall, Jean
http://library.link/vocab/subjectName
  • Sulfur
  • Sulfur bacteria
  • Sulfur cycle
  • Sulfur
  • Oxidation-Reduction
  • Sulfur-Reducing Bacteria
  • Soufre
  • Sulfobactéries
  • Cycle du soufre
  • Sulfur bacteria
  • Sulfur cycle
  • Sulfur
  • Micro-organismen
  • Zwavelverbindingen
  • Stofwisseling
  • Enzymologia
  • Siarka
  • Mikroorganismus
  • Schwefelstoffwechsel
  • Anorganische Verbindungen
  • Stickstoffverbindungen
  • Stoffwechsel
  • Aufsatzsammlung
Label
Inorganic microbial sulfur metabolism, edited by Harry D. Peck, Jr., Jean LeGall
Instantiates
Publication
Note
Founding editors: Sidney P. Colowick and Nathan O. Kaplan
Bibliography note
Includes bibliographical references and indexes
Carrier category
volume
Carrier category code
nc
Carrier MARC source
rdacarrier
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Contents
  • 5. Nickel-Iron Hydrogenase
  • Richard Cammack, Victor M. Fernandez Lopez and E. Claude Hatchikian
  • 6. Nickel-Iron-Selenium Hydrogenase
  • Daulat S. Patil
  • 7. The Pyruvic Acid Phosphoroclastic Reaction
  • Larry L. Barton
  • 8. Monoheme Cytochromes
  • Tatsuhiko Yagi
  • 9. Tetraheme Cytochromes
  • Isabel B. Coutinho and Antonio V. Xavier
  • 1. Sulfate Transport
  • 10. Cytochrome c[subscript 3] (M[subscript r] 26,000) Isolated from Sulfate-Reducing Bacteria and Its Relationships to Other Polyhemic Cytochromes from Desulfovibrio
  • Mireille Bruschi
  • 11. Hexadecaheme Cytochrome c
  • Yoshiki Higuchi, Tatsuhiko Yagi and Gerrit Voordouw
  • Heribert Cypionka
  • 2. NAD-Dependent Alcohol Dehydrogenase from Desulfovibrio gigas
  • Theo A. Hansen and Charles M.H. Hensgens
  • 3. NAD(P)-Independent Lactate Dehydrogenase from Sulfate-Reducing Prokaryotes
  • Theo A. Hansen
  • 4. Aldehyde Oxidoreductases and Other Molybdenum-Containing Enzymes
  • Jose J.G. Moura and Belarmino A.S. Barata
  • 16. Adenylylsulfate Reductases from Sulfate-Reducing Bacteria
  • Jorge Lampreia, Alice S. Pereira and Jose J.G. Moura
  • 17. Thiosulfate and Trithionate Reductases
  • J.M. Akagi, H.L. Drake, Jae-Ho Kim and Diane Gevertz
  • 18. Desulforubidin: Dissimilatory, High-Spin Sulfite Reductase of Desulfomicrobium Species
  • Daniel V. DerVartanian
  • 19. Desulfofuscidin: Dissimilatory, High-Spin Sulfite Reductase of Thermophilic, Sulfate-Reducing Bacteria
  • E. Claude Hatchikian
  • 20. Low-Spin Sulfite Reductases
  • Isabel Moura and Ana Rosa Lino
  • 12. Ferredoxins
  • Jose J.G. Moura, Anjos L. Macedo and P. Nuno Palma
  • 13. Flavodoxins
  • Jacques Vervoort, Dirk Heering, Sjaak Peelen and Willem van Berkel
  • 14. Rubredoxin in Crystalline State
  • Larry C. Sieker, Ronald E. Stenkamp and Jean LeGall
  • 15. Characterization of Three Proteins Containing Multiple Iron Sites: Rubrerythrin, Desulfoferrodoxin, and a Protein Containing a Six-Iron Cluster
  • Isabel Moura, Pedro Tavares and Natarajan Ravi
  • 25. Sulfur Reductases from Spirilloid Mesophilic Sulfur-Reducing Eubacteria
  • Guy D. Fauque, Oliver Klimmek and Achim Kroger
  • 26. Purification of Rusticyanin, a Blue Copper Protein from Thiobacillus ferrooxidans
  • John W. Ingledew and D.H. Boxer
  • 27. Adenylylsulfate Reductases from Thiobacilli
  • Barrie F. Taylor
  • 28. Enzymes of Dissimilatory Sulfide Oxidation in Phototrophic Sulfur Bacteria
  • Christiane Dahl and Hans G. Truper
  • 21. Hexaheme Nitrite Reductase from Desulfovibrio desulfuricans (ATCC 27774)
  • Ming-Cheh Liu, Cristina Costa and Isabel Moura
  • 22. Genetic Manipulation of Desulfovibrio
  • Walter M.A.M. van Dongen, Jack P.W.G. Stokkermans and Willy A.M. van den Berg
  • 23. Enzymology and Molecular Biology of Sulfate Reduction in the Extremely Thermophilic Archeon Archaeoglobus fulgidus
  • Christiane Dahl, Norbert Speich and Hans G. Truper
  • 24. Sulfur Reductase from Thiophilic Sulfate-Reducing Bacteria
  • Guy D. Fauque
  • 33. Sulfur-Oxidizing Enzymes
  • Isamu Suzuki
  • 34. Sulfide-Cytochrome c Reductase (Flavocytochrome c)
  • Tateo Yamanaka
  • 35. Synthesis and Determination of Thiosulfate and Polythionates
  • Don P. Kelly and Ann P. Wood
  • 36. Enzymes Involved in the Microbiological Oxidation of Thiosulfate and Polythionates
  • Don P. Kelly and Ann P. Wood
  • 37. Whole-Organism Methods for Inorganic Sulfur Oxidation by Chemolithotrophs and Photolithotrophs
  • Don P. Kelly and Ann P. Wood
  • 29. Reverse Siroheme Sulfite Reductase from Thiobacillus denitrificans
  • 38. Mossbauer Spectroscopy in Study of Cytochrome cd[subscript 1] from Thiobacillus denitrificans, Desulfoviridin, and Iron Hydrogenase
  • Boi Hanh Huynh
  • Hans G. Truper
  • 30. Purification and Properties of Cytochrome c-555 from Phototrophic Green Sulfur Bacteria
  • T.E. Meyer
  • 31. Purification and Properties of High-Potential Iron-Sulfur Proteins
  • T.E. Meyer
  • 32. Sulfite: Cytochrome c Oxidoreductase of Thiobacilli
  • Isamu Suzuki
  • 39. In Vivo Nuclear Magnetic Resonance in Study of Physiology of Sulfate-Reducing Bacteria
  • Helena Santos, Paula Fareleira, Jean LeGall and Antonio V. Xavier
  • 40. Computational Chemistry and Molecular Modeling of Electron-Transfer Proteins
  • John E. Wampler
  • 41. Immunoassay of Sulfate-Reducing Bacteria in Environmental Samples
  • J. Martin Odom and Richard C. Ebersole
Extent
xxix, 682 pages
Isbn
9780121821449
Media category
unmediated
Media MARC source
rdamedia
Media type code
n
Other physical details
illustrations.
System control number
  • (OCoLC)31229357
  • (OCoLC)ocm31229357
Label
Inorganic microbial sulfur metabolism, edited by Harry D. Peck, Jr., Jean LeGall
Publication
Note
Founding editors: Sidney P. Colowick and Nathan O. Kaplan
Bibliography note
Includes bibliographical references and indexes
Carrier category
volume
Carrier category code
nc
Carrier MARC source
rdacarrier
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Contents
  • 5. Nickel-Iron Hydrogenase
  • Richard Cammack, Victor M. Fernandez Lopez and E. Claude Hatchikian
  • 6. Nickel-Iron-Selenium Hydrogenase
  • Daulat S. Patil
  • 7. The Pyruvic Acid Phosphoroclastic Reaction
  • Larry L. Barton
  • 8. Monoheme Cytochromes
  • Tatsuhiko Yagi
  • 9. Tetraheme Cytochromes
  • Isabel B. Coutinho and Antonio V. Xavier
  • 1. Sulfate Transport
  • 10. Cytochrome c[subscript 3] (M[subscript r] 26,000) Isolated from Sulfate-Reducing Bacteria and Its Relationships to Other Polyhemic Cytochromes from Desulfovibrio
  • Mireille Bruschi
  • 11. Hexadecaheme Cytochrome c
  • Yoshiki Higuchi, Tatsuhiko Yagi and Gerrit Voordouw
  • Heribert Cypionka
  • 2. NAD-Dependent Alcohol Dehydrogenase from Desulfovibrio gigas
  • Theo A. Hansen and Charles M.H. Hensgens
  • 3. NAD(P)-Independent Lactate Dehydrogenase from Sulfate-Reducing Prokaryotes
  • Theo A. Hansen
  • 4. Aldehyde Oxidoreductases and Other Molybdenum-Containing Enzymes
  • Jose J.G. Moura and Belarmino A.S. Barata
  • 16. Adenylylsulfate Reductases from Sulfate-Reducing Bacteria
  • Jorge Lampreia, Alice S. Pereira and Jose J.G. Moura
  • 17. Thiosulfate and Trithionate Reductases
  • J.M. Akagi, H.L. Drake, Jae-Ho Kim and Diane Gevertz
  • 18. Desulforubidin: Dissimilatory, High-Spin Sulfite Reductase of Desulfomicrobium Species
  • Daniel V. DerVartanian
  • 19. Desulfofuscidin: Dissimilatory, High-Spin Sulfite Reductase of Thermophilic, Sulfate-Reducing Bacteria
  • E. Claude Hatchikian
  • 20. Low-Spin Sulfite Reductases
  • Isabel Moura and Ana Rosa Lino
  • 12. Ferredoxins
  • Jose J.G. Moura, Anjos L. Macedo and P. Nuno Palma
  • 13. Flavodoxins
  • Jacques Vervoort, Dirk Heering, Sjaak Peelen and Willem van Berkel
  • 14. Rubredoxin in Crystalline State
  • Larry C. Sieker, Ronald E. Stenkamp and Jean LeGall
  • 15. Characterization of Three Proteins Containing Multiple Iron Sites: Rubrerythrin, Desulfoferrodoxin, and a Protein Containing a Six-Iron Cluster
  • Isabel Moura, Pedro Tavares and Natarajan Ravi
  • 25. Sulfur Reductases from Spirilloid Mesophilic Sulfur-Reducing Eubacteria
  • Guy D. Fauque, Oliver Klimmek and Achim Kroger
  • 26. Purification of Rusticyanin, a Blue Copper Protein from Thiobacillus ferrooxidans
  • John W. Ingledew and D.H. Boxer
  • 27. Adenylylsulfate Reductases from Thiobacilli
  • Barrie F. Taylor
  • 28. Enzymes of Dissimilatory Sulfide Oxidation in Phototrophic Sulfur Bacteria
  • Christiane Dahl and Hans G. Truper
  • 21. Hexaheme Nitrite Reductase from Desulfovibrio desulfuricans (ATCC 27774)
  • Ming-Cheh Liu, Cristina Costa and Isabel Moura
  • 22. Genetic Manipulation of Desulfovibrio
  • Walter M.A.M. van Dongen, Jack P.W.G. Stokkermans and Willy A.M. van den Berg
  • 23. Enzymology and Molecular Biology of Sulfate Reduction in the Extremely Thermophilic Archeon Archaeoglobus fulgidus
  • Christiane Dahl, Norbert Speich and Hans G. Truper
  • 24. Sulfur Reductase from Thiophilic Sulfate-Reducing Bacteria
  • Guy D. Fauque
  • 33. Sulfur-Oxidizing Enzymes
  • Isamu Suzuki
  • 34. Sulfide-Cytochrome c Reductase (Flavocytochrome c)
  • Tateo Yamanaka
  • 35. Synthesis and Determination of Thiosulfate and Polythionates
  • Don P. Kelly and Ann P. Wood
  • 36. Enzymes Involved in the Microbiological Oxidation of Thiosulfate and Polythionates
  • Don P. Kelly and Ann P. Wood
  • 37. Whole-Organism Methods for Inorganic Sulfur Oxidation by Chemolithotrophs and Photolithotrophs
  • Don P. Kelly and Ann P. Wood
  • 29. Reverse Siroheme Sulfite Reductase from Thiobacillus denitrificans
  • 38. Mossbauer Spectroscopy in Study of Cytochrome cd[subscript 1] from Thiobacillus denitrificans, Desulfoviridin, and Iron Hydrogenase
  • Boi Hanh Huynh
  • Hans G. Truper
  • 30. Purification and Properties of Cytochrome c-555 from Phototrophic Green Sulfur Bacteria
  • T.E. Meyer
  • 31. Purification and Properties of High-Potential Iron-Sulfur Proteins
  • T.E. Meyer
  • 32. Sulfite: Cytochrome c Oxidoreductase of Thiobacilli
  • Isamu Suzuki
  • 39. In Vivo Nuclear Magnetic Resonance in Study of Physiology of Sulfate-Reducing Bacteria
  • Helena Santos, Paula Fareleira, Jean LeGall and Antonio V. Xavier
  • 40. Computational Chemistry and Molecular Modeling of Electron-Transfer Proteins
  • John E. Wampler
  • 41. Immunoassay of Sulfate-Reducing Bacteria in Environmental Samples
  • J. Martin Odom and Richard C. Ebersole
Extent
xxix, 682 pages
Isbn
9780121821449
Media category
unmediated
Media MARC source
rdamedia
Media type code
n
Other physical details
illustrations.
System control number
  • (OCoLC)31229357
  • (OCoLC)ocm31229357

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