000 | 07015cam a2200841 i 4500 | ||
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001 | 34500 | ||
003 | OCoLC | ||
005 | 20250813105631.0 | ||
006 | m o d | ||
007 | cr cn||||||||| | ||
008 | 140901t20152015gw a ob 001 0 eng d | ||
016 | 7 |
_a019195053 _2Uk |
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020 |
_a9783527664184 _q(e-book) |
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020 |
_a9783527333080 _q(e-book) |
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029 | 1 |
_aAU@ _b000053548470 |
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_aCHBIS _b010259810 |
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_aCHNEW _b000943579 |
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035 |
_a(OCoLC)891398199 _z(OCoLC)961515426 _z(OCoLC)962633651 _z(OCoLC)1069592851 |
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037 |
_a9783527664184 _bWiley |
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040 |
_aE7B _beng _erda _epn _cمكتبة قسم علوم الحياة |
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050 | 4 |
_aQD474 _b.B565 2015eb |
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082 | 0 | 4 |
_a541.3 _223 _bW;415 |
100 |
_qWeigand,Wolfgang _eEdited |
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245 | 0 | 0 |
_aBioinspired catalysis = _bmetal-sulfur complexes / _cedited by Wolfgang Weigand and Philippe Schollhammer ; contributors Ulf-Peter Apfel [and thirty three others]. |
264 | 1 |
_aWeinheim, Germany : _bWiley-VCH, _c2015. |
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264 | 4 | _c�2015 | |
300 |
_a1 online resource (438 pages) : _billustrations _c24cm |
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336 |
_atext _btxt _2rdacontent |
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337 |
_acomputer _bc _2rdamedia |
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338 |
_aonline resource _bcr _2rdacarrier |
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440 | _aBioinspired catalysis | ||
500 | _aThe growing interest in green chemistry calls for new efficient and cheap catalysts | ||
504 | _aIncludes bibliographical references at the end of each chapters and index. | ||
505 | 0 | _aRelated Titles; Title Page; Copyright; List of Contributors; Preface; Part I: PrimordialMetal-Sulfur-Mediated Reactions; Chapter 1: From Chemical Invariance to Genetic Variability; 1.1 Heuristic of Biochemical Retrodiction; 1.2 Retrodicting the Elements of Life; 1.3 Retrodicting Pioneer Catalysis; 1.4 Retrodicting Metabolic Reproduction and Evolution; 1.5 Retrodicting Pioneer-Metabolic Reactions; 1.6 Early Evolution in a Spatiotemporal Flow Context; Acknowledgments; References; Chapter 2: Fe-S Clusters: Biogenesis and Redox, Catalytic, and Regulatory Properties; 2.1 Introduction. | |
505 | 8 | _a2.2 Fe-S Cluster Biogenesis and Trafficking2.3 Redox Properties of Fe-S Clusters; 2.4 Fe-S Clusters and Catalysis; 2.5 Fe-S Clusters and Oxidative Stress; 2.6 Regulation of Protein Expression by Fe-S Clusters; 2.7 Conclusion; References; Part II: Model Complexes of the Active Site of Hydrogenases -- Proton and Dihydrogen Activation; Chapter 3: [NiFe] Hydrogenases; 3.1 Introduction; 3.2 Introduction to [NiFe] Hydrogenases; 3.3 Nickel Thiolate Complexes as Analogs of [NiFe] Hydrogenase; 3.4 [NiFe] Hydrogenase Model Complexes; 3.5 Analogs of [NiFe] Hydrogenase Incorporating Proton Relays. | |
505 | 8 | _a3.6 Perspectives and Future ChallengesAcknowledgments; References; Chapter 4: [FeFe] Hydrogenase Models: an Overview; 4.1 Introduction; 4.2 Synthetic Strategies toward [FeFe] Hydrogenase Model Complexes; 4.3 Properties of Model Complexes; 4.4 Conclusion; References; Chapter 5: The Third Hydrogenase; 5.1 Introduction; 5.2 Initial Studies of Hmd; 5.3 Discovery that Hmd Contains a Bound Cofactor; 5.4 Discovery that Hmd is a Metalloenzyme; 5.5 Crystal Structure Studies of [Fe] Hydrogenase; 5.6 Mechanistic Models of [Fe] Hydrogenase; References. | |
505 | 8 | _aChapter 6: DFT Investigation of Models Related to the Active Site of Hydrogenases6.1 Introduction; 6.2 QM Studies of Hydrogenases; 6.3 QM Studies of Synthetic Complexes Related to the Active Site of Hydrogenases; 6.4 Conclusions; References; Chapter 7: Mechanistic Aspects of Biological Hydrogen Evolution and Uptake; 7.1 Introduction; 7.2 [FeFe] Hydrogenases; 7.3 [NiFe] Hydrogenases; 7.4 [Fe] Hydrogenase; 7.5 Nitrogenase; References; Part III: Nitrogen Fixation; Chapter 8: Structures and Functions of the Active Sites of Nitrogenases; 8.1 Introduction; 8.2 Properties of Mo Nitrogenase. | |
505 | 8 | _a8.3 Catalysis by Mo Nitrogenase8.4 Unique Features of V Nitrogenase; 8.5 Catalytic Properties of Isolated FeMo-co and FeVco; Acknowledgments; References; Chapter 9: Model Complexes of the Active Site of Nitrogenases: Recent Advances; 9.1 Introduction; 9.2 Structural Models of Metal-Sulfur Clusters in the Nitrogenases; 9.3 Functional Modeling at a Single Molybdenum Center; 9.4 Functional Modeling at a Single Iron Center; 9.5 The Hydrogen and Homocitrate Issues in Nitrogenase Model Chemistry; 9.6 Sulfur- and Metal-Metal Interaction in Functional Models of Nitrogenase. | |
520 | _aThis book provides an overview of bioinspired metal-sulfur catalysis by covering structures, activities and model complexes of enzymes exhibiting metal sulphur moieties in their active center. | ||
588 | 0 | _aOnline resource; title from PDF title page (ebrary, viewed August 30, 2014). | |
650 | 0 | _aMetal complexes. | |
650 | 6 | _aComplexes m�etalliques. | |
650 | 7 |
_aSCIENCE _xChemistry _xInorganic. _2bisacsh |
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650 | 7 |
_aBiochemistry. _2bisacsh/2022 |
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650 | 7 |
_aLife Sciences. _2bisacsh/2022 |
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650 | 7 |
_aSCIENCE. _2bisacsh/2022 |
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650 | 7 |
_aMetal complexes _2fast |
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655 | 0 | _aElectronic books. | |
700 | 1 |
_aWeigand, Wolfgang, _eeditor. |
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700 | 1 |
_aSchollhammer, Philippe, _eeditor. |
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700 | 1 |
_aApfel, Ulf-Peter, _econtributor. |
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776 | 0 | 8 |
_iPrint version: _tBioinspired catalysis : metal-sulfur complexes. _dWeinheim, Germany : Wiley-VCH, �2015 _hxviii, 417 pages _z9783527333080 |
856 | 4 | 0 |
_3ebrary _uhttp://site.ebrary.com/id/10909194 |
856 | 4 | 0 |
_3ProQuest Ebook Central _uhttps://public.ebookcentral.proquest.com/choice/publicfullrecord.aspx?p=1767040 |
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_3Wiley _uhttps://doi.org/10.1002/9783527664160 |
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_3Wiley _uhttps://onlinelibrary.wiley.com/doi/book/10.1002/9783527664160 |
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_3Front cover, high quality _uhttps://images.yourcloudlibrary.com/delivery/img?type=DOCUMENTIMAGE&documentID=eugpx89&size=ORIGINAL |
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910 | _aمها ازاد حامد | ||
936 | _aBATCHLOAD | ||
942 |
_2ddc _cBK |
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948 | _hNO HOLDINGS IN IQMCL - 263 OTHER HOLDINGS | ||
999 |
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