Bioinorganic CatalysisJan Reedijk, Elisabeth Bouwman CRC Press, 2. 2. 1999 - Počet stran: 624 "Provides the latest research results and suggests new topics for interdisciplinary study of metal ions, catalysis, and biochemical systems. Second Edition highlights potential applications; includes new chapters on zinc and FeS clusters; presents new X-ray analysis of metalloenzymes; and more." |
Vyhledávání v knize
Výsledky 1-5 z 67
Strana vi
... Copper Dioxygen Complexes 469 Kenneth D. Karlin and Andreas D. Zuberbühler 15. Multielectron Transfer and Catalytic Mechanisms in Oxidative Polymerization 535 Eishun Tsuchida , Kimihisa Yamamoto , and Kenichi Oyaizu 16. Metalloenzymes ...
... Copper Dioxygen Complexes 469 Kenneth D. Karlin and Andreas D. Zuberbühler 15. Multielectron Transfer and Catalytic Mechanisms in Oxidative Polymerization 535 Eishun Tsuchida , Kimihisa Yamamoto , and Kenichi Oyaizu 16. Metalloenzymes ...
Strana 1
... copper , manganese , and zinc , has only been known for more than half a century . It has also been known for a long time that an excess of these elements can be very dangerous , and , as a matter of fact , a narrow concentration window ...
... copper , manganese , and zinc , has only been known for more than half a century . It has also been known for a long time that an excess of these elements can be very dangerous , and , as a matter of fact , a narrow concentration window ...
Strana 3
... Copper 100 3 X 10-1 2 Zinc 2000 4 X 10-1 12 Manganese 20 2 × 10-2 3 Molybdenum 5 10 0.2 Cobalt 1 1 X 10-3 0.3 Selenium 0.5 2 × 10-1 0.1 Magnesium 4 X 104 106 350 Calcium 106 4 X 105 800 Nickel < 0.1 5 × 10-1 < 0.1 Some comments about ...
... Copper 100 3 X 10-1 2 Zinc 2000 4 X 10-1 12 Manganese 20 2 × 10-2 3 Molybdenum 5 10 0.2 Cobalt 1 1 X 10-3 0.3 Selenium 0.5 2 × 10-1 0.1 Magnesium 4 X 104 106 350 Calcium 106 4 X 105 800 Nickel < 0.1 5 × 10-1 < 0.1 Some comments about ...
Strana 5
... copper ion in blue cop- per enzymes facilitates the redox switches of the copper ion , which otherwise would require a significant change in geometry . For the bioinorganic chemists who are trying to mimic the activity of metal ...
... copper ion in blue cop- per enzymes facilitates the redox switches of the copper ion , which otherwise would require a significant change in geometry . For the bioinorganic chemists who are trying to mimic the activity of metal ...
Strana 8
... copper trans- port , and ferritin for iron storage . In addition to these natural transporting pro- teins , nature makes use of other systems to remove excess of toxic metal ions . The metallothionines , for example , take care of ...
... copper trans- port , and ferritin for iron storage . In addition to these natural transporting pro- teins , nature makes use of other systems to remove excess of toxic metal ions . The metallothionines , for example , take care of ...
Obsah
1 | |
13 | |
23 | |
33 | |
Vanadium Haloperoxidases | 55 |
Molybdenum and Tungsten Enzymes | 81 |
Catalysis by Nitrogenases and Synthetic Analogs | 153 |
Biological IronSulfur Clusters with Catalytic Activity | 209 |
Dioxygen Activation at Heme Centers in Enzymes and Synthetic Analogs | 323 |
Biological and Biomimetic Catalysis of Manganese Redox Enzymes and Their Inorganic Models | 355 |
The Two B12 Cofactors Influence of the trans Nitrogen Ligand on Homolytic and Heterolytic Processes | 423 |
Formation Structure and Reactivity of Copper Dioxygen Complexes | 469 |
Multielectron Transfer and Catalytic Mechanisms in Oxidative Polymerization | 535 |
Metalloenzymes with a Quinone Cofactor | 563 |
Future Developments | 587 |
Index | 595 |
Catalysis by Nickel in Biological Systems | 231 |
Oxygen Activation at NonhemeIron Centers | 269 |
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acid Acta active active site amine analogs axial bacteria binding Biochem Biochemistry bioinorganic Biol biological Biophys bridging bromination carbon catalase catalysis catalytic cycle Chem chemistry cleavage cluster Co-C bond coenzyme cofactor complex compounds coordination copper coupling crystal structure cytochrome P-450 dehydrogenase dihydrogen peroxide dinuclear dioxygen dioxygenases dmso donor electron transfer enzyme EXAFS Fe protein Fe(II FeMoco Figure formation H₂ H₂O heme histidine homolysis hydrogen hydrogenases hydrolysis hydron hydroxylation imidazole Inorg intermediate involved iron iron-sulfur iron(III K.D. Karlin kinetic L.G. Marzilli ligand mechanism metal center metal ions methyl Mn"Mn molecule molybdenum molybdenum and tungsten N₂ nickel nitrogen nitrogenase O₂ observed oxidation oxido oxygen atom peroxo phenol polymerization porphyrin proposed protein radical reaction reactivity redox reductase reduction residue role Scheme species spectroscopic studies substrate subunit suggest sulfur superoxide thiolate tion V-BrPO x-ray xanthine oxidase