Molybdenum enzymes, cofactors, and model systems : developed from a symposium sponsored by the Division of Inorganic Chemistry at the 204th National Meeting of the American Chemical Society, Washington, DC, August 23-28, 1992 / Edward I. Stiefel, editor, Dimitri Coucouvanis, editor, William E. Newton, editor
| Medienart: |
E-Book |
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| Erscheinungsjahr: |
1993 |
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| Erschienen: |
Washington, DC: American Chemical Society ; 1993 |
| Reihe: |
ACS symposium series - 535 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Stiefel, Edward I., 1942- [HerausgeberIn] |
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| Congresses: |
American Chemical Society ; (204th ; Washington, D.C.) ; 1992 ; Meeting |
| Links: |
pubs.acs.org [lizenzpflichtig] |
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| ISBN: |
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| Anmerkungen: |
Distributed in print by Oxford University Press Includes bibliographical references and index |
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| Umfang: |
1 Online-Ressource (412 pages) ; illustrations |
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| doi: |
10.1021/bk-1993-0535 |
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| Weitere IDs: |
bk-1993-0535 |
| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
1841190500 |
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| 245 | 1 | 0 | |a Molybdenum enzymes, cofactors, and model systems |b developed from a symposium sponsored by the Division of Inorganic Chemistry at the 204th National Meeting of the American Chemical Society, Washington, DC, August 23-28, 1992 |c Edward I. Stiefel, editor, Dimitri Coucouvanis, editor, William E. Newton, editor |
| 264 | 1 | |a Washington, DC |b American Chemical Society |c 1993 | |
| 300 | |a 1 Online-Ressource (412 pages) |b illustrations | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 490 | 0 | |a ACS symposium series |v 535 | |
| 500 | |a Distributed in print by Oxford University Press | ||
| 500 | |a Includes bibliographical references and index | ||
| 505 | 8 | 0 | |t Molybdenum Enzymes, Cofactors, and Chemistry: An Introductory Survey / |r Stiefel, Edward I. / |
| 505 | 8 | 0 | |t The Reaction Mechanism of Xanthine Oxidase / |r Hille, Russ / |
| 505 | 8 | 0 | |t Biochemistry of the Molybdenum Cofactors / |r Rajagopalan, K. V. / |
| 505 | 8 | 0 | |t The Bacterial Molybdenum Cofactor / |r Meyer, O.; Frunzke, K.; Tachil, J.; Volk, M. / |
| 505 | 8 | 0 | |t Models of Pterin-Containing Molybdenum Enzymes / |r Young, Charles G.; Wedd, Anthony G. / |
| 505 | 8 | 0 | |t Pterins, Quinoxalines, and Metallo-Ene-Dithiolates: Synthetic Approach to the Molybdenum Cofactor / |r Pilato, Robert S., Exxon Research and Engineering Company, Clinton Township, Route 22 East, Annandale, NJ 08801, Current address: Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742; Eriksen, K., Exxon Research and Engineering Company, Clinton Township, Route 22 East, Annandale, NJ 08801; Greaney, M. A., Exxon Research and Engineering Company, Clinton Township, Route 22 East, Annandale, NJ 08801; Gea, Y., Exxon Research and Engineering Company, Clinton Township, Route 22 East, Annandale, NJ 08801; Taylor, E. C., Department of Chemistry, Princeton University, Princeton, NJ 08540; Goswami, S., Department of Chemistry, Princeton University, Princeton, NJ 08540; Kilpatrick, L., Department of Chemistry, Princeton University, Princeton, NJ 08540; Spiro, T. G., Department of Chemistry, Princeton University, Princeton, NJ 08540; Rheingold, A. L., Department of Chemistry, University of Delaware, Newark, DE 19711; Stiefel, Edward I., Exxon Research and Engineering Company, Clinton Township, Route 22 East, Annandale, NJ 08801 / |
| 505 | 8 | 0 | |t Strategies for the Synthesis of the Cofactor of the Oxomolybdoenzymes / |r Garner, C. D.; Armstrong, E. M.; Ashcroft, M. J.; Austerberry, M. S.; Birks, J. H.; Collison, D.; Goodwin, A. J.; Larsen, L.; Rowe, D. J.; Russell, J. R. / |
| 505 | 8 | 0 | |t Molybdenum Complexes of Reduced Pterins / |r Nieter Burgmayer, Sharon J.; Everett, Kristin; Bostick, Laura / |
| 505 | 8 | 0 | |t Chemical and Physical Coupling of Oxomolybdenum Centers and Iron Porphyrins: Models for the Molybdenum—Iron Interaction in Sulfite Oxidase / |r LaBarre, Michael J.; Raitsimring, Arnold; Enemark, John H. / |
| 505 | 8 | 0 | |t Nitrogenase Structure, Function, and Genetics / |r Burgess, Barbara K. / |
| 505 | 8 | 0 | |t Crystal Structures of the Iron Protein and Molybdenum—Iron Protein of Nitrogenase / |r Rees, D. C., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125; Kim, J., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125; Georgiadis, M. M., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, Current address: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032; Komiya, H., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125; Chirino, A. J., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125; Woo, D., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125; Schlessman, J., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125; Chan, M. K., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125; Joshua-Tor, L., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125; Santillan, G., Department of Chemistry, California State University Los Angeles, CA 91030; Chakrabarti, P., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, Current address: Physical Chemistry Division, National Chemical Laboratory, Pune 411008, India; Hsu, B. T., Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125 / |
| 505 | 8 | 0 | |t Structure and Environment of Metal Clusters in the Nitrogenase Molybdenum—Iron Protein from Clostridium pasteurianum / |r Bolin, Jeffrey T., Department of Biological Sciences, Purdue University, West Lafayette, IN 47907; Campobasso, Nino, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907; Muchmore, Steven W., Department of Biological Sciences, Purdue University, West Lafayette, IN 47907; Morgan, T. Vance, Center for Metalloenzyme Studies, Department of Biochemistry, University of Georgia, Athens, GA 30602; Mortenson, Leonard E., Center for Metalloenzyme Studies, Department of Biochemistry, University of Georgia, Athens, GA 30602 / |
| 505 | 8 | 0 | |t Biosynthesis of the Iron—Molybdenum Cofactor of Nitrogenase / |r Ludden, Paul W., Department of Biochemistry, University of Wisconsin, Madison, WI 53706; Shah, Vinod K., Department of Biochemistry, University of Wisconsin, Madison, WI 53706; Roberts, Gary P., Department of Bacteriology, University of Wisconsin, Madison, WI 53706; Homer, Mary, Department of Bacteriology, University of Wisconsin, Madison, WI 53706; Allen, Ronda, Department of Biochemistry, University of Wisconsin, Madison, WI 53706; Paustian, Tim, Department of Bacteriology, University of Wisconsin, Madison, WI 53706; Roll, Jon, Department of Bacteriology, University of Wisconsin, Madison, WI 53706; Chatterjee, Ranjini, Department of Biochemistry, University of Wisconsin, Madison, WI 53706; Madden, Mark, Department of Biochemistry, University of Wisconsin, Madison, WI 53706; Allen, Jeff, Department of Biochemistry, University of Wisconsin, Madison, WI 53706 / |
| 505 | 8 | 0 | |t Role of the Iron—Molybdenum Cofactor Polypeptide Environment in Azotobacter vinelandii Molybdenum—Nitrogenase Catalysis / |r Newton, William E., Department of Biochemistry and Nutrition, Virginia Polytechnic Institute & State University, Blacksburg, VA 24061-0308; Dean, Dennis R., Department of Anaerobic Microbiology, Virginia Polytechnic Institute & State University, Blacksburg, VA 24061-0305 / |
| 505 | 8 | 0 | |t Extended X-ray Absorption Fine Structure and L-Edge Spectroscopy of Nitrogenase Molybdenum—Iron Protein / |r Chen, J., Energy and Environment Division, Lawrence Berkeley Laboratory, Berkeley, CA 94720; Christiansen, J., Department of Applied Science, University of California, Davis, CA 95616; George, S. J., Department of Applied Science, University of California, Davis, CA 95616; van Elp, J., Energy and Environment Division, Lawrence Berkeley Laboratory, Berkeley, CA 94720; Tittsworth, R., Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803; Hales, B. J., Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803; Al-Ahmad, S., Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055; Coucouvanis, Dimitri, Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055; Campobasso, Nino, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907; Bolin, Jeffrey T., Department of Biological Sciences, Purdue University, West Lafayette, IN 47907; Cramer, S. P., Energy and Environment Division, Lawrence Berkeley Laboratory, Berkeley, CA 94720, Department of Applied Science, University of California, Davis, CA 95616 / |
| 505 | 8 | 0 | |t Redox Properties of the Nitrogenase Proteins from Azotobacter vinelandii / |r Watt, G. D., Department of Chemistry, Brigham Young University, Provo, UT 84602; Huang, H., Department of Biology, Xiamen University, Xiamen, People's Republic of China; Reddy, K. R. N., Department of Chemistry, University of Maryland, Baltimore, MD 21228 / |
| 505 | 8 | 0 | |t The Molybdenum—Iron Protein of Nitrogenase: Structural and Functional Features of Metal Cluster Prosthetic Groups / |r Orme-Johnson, W. H. / |
| 505 | 8 | 0 | |t Protein Component Complex Formation and Adenosine Triphosphate Hydrolysis in Nitrogenase / |r Howard, James Bryant / |
| 505 | 8 | 0 | |t Electron-Transfer Reactions Associated with Nitrogenase from Klebsiella pneumoniae / |r Thorneley, R. N. F.; Ashby, G. A.; Fisher, K.; Lowe, D. J. / |
| 505 | 8 | 0 | |t Recent Structure Determinations of the Molybdenum—Iron Protein of Nitrogenase: Impact on Design of Synthetic Analogs for the Iron-Molybdenum-Sulfur Active Site and the Iron—Molybdenum Cofactor / |r Coucouvanis, Dimitri / |
| 505 | 8 | 0 | |t Bonding, Activation, and Stabilization of Small Molecules by Molybdenum—Sulfur and Iron—Sulfur Systems / |r Sellmann, Dieter / |
| 505 | 8 | 0 | |t Chemical Transformations of Coordinated Dinitrogen in Molybdenum and Tungsten Phosphine Complexes / |r Hidai, Masanobu; Mizobe, Yasushi / |
| 650 | 0 | |a Molybdenum enzymes | |
| 650 | 0 | |a Coenzymes | |
| 650 | 0 | |a Xanthine oxidase |x Mechanism of action | |
| 650 | 0 | |a Molybdenum enzymes |x Properties | |
| 650 | 0 | |a Biochemistry | |
| 650 | 0 | |a Molybdenum enzymes |x Computer simulation | |
| 650 | 0 | |a Molybdenum enzymes |x Synthesis | |
| 650 | 0 | |a Pteridines | |
| 650 | 0 | |a Iron-molybdenum alloys |x Reactivity | |
| 650 | 0 | |a Nitrogenase |x Analysis | |
| 650 | 0 | |a Iron-molybdenum alloys |x Structure | |
| 650 | 0 | |a Iron-molybdenum alloys |x Synthesis | |
| 650 | 0 | |a Nitrogenase |x Synthesis | |
| 650 | 0 | |a Polypeptides | |
| 650 | 0 | |a Iron-molybdenum alloys |x Analysis |x Methodology | |
| 650 | 0 | |a X-ray spectroscopy | |
| 650 | 0 | |a Spectrum analysis | |
| 650 | 0 | |a Azotobacter vinelandii |x Properties | |
| 650 | 0 | |a Metal clusters |x Structure | |
| 650 | 0 | |a Adenosine triphosphate | |
| 650 | 0 | |a Oxidation-reduction reaction | |
| 650 | 0 | |a Klebsiella pneumoniae | |
| 650 | 0 | |a Iron-sulfur proteins |x Molecular aspects | |
| 650 | 0 | |a Chemical reactions | |
| 650 | 0 | |a Molybdenum compounds | |
| 650 | 0 | |a Tungsten compounds | |
| 650 | 2 | |a Molybdenum |x chemistry | |
| 650 | 2 | |a Enzymes |x chemistry | |
| 650 | 2 | |a Xanthine Oxidase |x chemistry | |
| 650 | 2 | |a Biochemical Phenomena | |
| 650 | 2 | |a Coenzymes |x chemistry | |
| 650 | 2 | |a Pterins |x chemistry | |
| 650 | 2 | |a Models, Chemical | |
| 650 | 2 | |a Quinoxalines |x chemistry | |
| 650 | 2 | |a Sulfite Oxidase |x chemistry | |
| 650 | 2 | |a Coenzymes |x chemical synthesis | |
| 650 | 2 | |a Nitrogenase |x genetics | |
| 650 | 2 | |a Nitrogenase |x analysis | |
| 650 | 2 | |a Proteins |x analysis | |
| 650 | 2 | |a Molybdoferredoxin |x analysis | |
| 650 | 2 | |a Clostridium |x chemistry | |
| 650 | 2 | |a Molybdoferredoxin |x biosynthesis | |
| 650 | 2 | |a Azotobacter vinelandii |x chemistry | |
| 650 | 2 | |a Biocatalysis | |
| 650 | 2 | |a X-Ray Absorption Spectroscopy | |
| 650 | 2 | |a Spectrum Analysis | |
| 650 | 2 | |a Oxidation-Reduction | |
| 650 | 2 | |a Adenosine Triphosphate |x chemistry | |
| 650 | 2 | |a Hydrolysis | |
| 650 | 2 | |a Klebsiella pneumoniae |x chemistry | |
| 650 | 2 | |a Sulfur Compounds |x chemistry | |
| 650 | 2 | |a Phosphines |x chemistry | |
| 650 | 2 | |a Tungsten Compounds |x chemistry | |
| 650 | 4 | |a SCIENCE / Life Sciences / Biochemistry | |
| 700 | 1 | |a Stiefel, Edward I. |d 1942- |e herausgeberin |4 edt | |
| 700 | 1 | |a Coucouvanis, Dimitri |d 1940- |e herausgeberin |4 edt | |
| 700 | 1 | |a Newton, William Edward |d 1938- |e herausgeberin |4 edt | |
| 710 | 2 | |a American Chemical Society |b Division of Inorganic Chemistry |e SponsorIn |4 spn | |
| 711 | 2 | |a American Chemical Society |e Meeting |n (204th |d 1992 |c Washington, D.C.) |4 oth | |
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