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Transition Metals in Catalysis: The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems

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Palabras clave – provistas por la editorial

CO dehydrogenase; dihydrogen; hydrogenase; quantum/classical modeling; density functional theory; metal–dithiolene; pyranopterin molybdenum enzymes; fold-angle; tungsten enzymes; electronic structure; pseudo-Jahn–Teller effect; thione; molybdenum cofactor; Moco; mixed-valence complex; dithiolene ligand; tetra-nuclear nickel complex; X-ray structure; magnetic moment; formate hydrogenlyase; hydrogen metabolism; energy conservation; MRP (multiple resistance and pH)-type Na+/H+ antiporter; CCCP—carbonyl cyanide m-chlorophenyl-hydrazone; EIPA—5-(N-ethyl-N-isopropyl)-amiloride; nicotinamide adenine dinucleotide (NADH); electron transfer; enzyme kinetics; enzyme structure; formate dehydrogenase; carbon assimilation; Moco biosynthesis; Fe-S cluster assembly; l-cysteine desulfurase; ISC; SUF; NIF; iron; molybdenum; sulfur; tungsten cofactor; aldehyde:ferredoxin oxidoreductase; benzoyl-CoA reductase; acetylene hydratase; [Fe]-hydrogenase; FeGP cofactor; guanylylpyridinol; conformational changes; X-ray crystallography; iron-sulfur cluster; persulfide; metallocofactor; frataxin; Friedreich’s ataxia; n/a

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Información

Tipo de recurso:

libros

ISBN electrónico

978-3-0365-0609-8

País de edición

Suiza