Transition Metals in Catalysis : The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems
Weitere Verfasser: |
Leimkühler, Silke
, [HerausgeberIn]
Magalon, Axel , [HerausgeberIn] Einsle, Oliver , [HerausgeberIn] Schulzke, Carola , [HerausgeberIn] |
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Umfang/Format: |
1 online resource (186 pages). |
Schlagworte: | |
Online Zugang: |
DOAB: download the publication DOAB: description of the publication |
LEADER | 03960namaa2201189ui 4500 | ||
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001 | 003028156 | ||
005 | 20221228154431.0 | ||
003 | DE-2553 | ||
006 | m o d | ||
007 | cr|mn|---annan | ||
008 | 20210501s2021 xx |||||o ||| 0|eng d | ||
020 | |a books978-3-0365-0609-8 | ||
020 | |a 9783036506081 | ||
020 | |a 9783036506098 | ||
040 | |a oapen |c oapen |b eng |d DE-2553 |e rda | ||
024 | 7 | |a 10.3390/books978-3-0365-0609-8 |c doi | |
041 | 0 | |a eng | |
042 | |a dc | ||
072 | 7 | |a GP |2 bicssc | |
072 | 7 | |a PS |2 bicssc | |
100 | 1 | |a Leimkühler, Silke |e editor | |
264 | |b MDPI - Multidisciplinary Digital Publishing Institute, |c 2021. | ||
700 | 1 | |a Magalon, Axel |e editor | |
700 | 1 | |a Einsle, Oliver |e editor | |
700 | 1 | |a Schulzke, Carola |e editor | |
700 | 1 | |a Leimkühler, Silke |e other | |
700 | 1 | |a Magalon, Axel |e other | |
700 | 1 | |a Einsle, Oliver |e other | |
700 | 1 | |a Schulzke, Carola |e other | |
245 | 1 | 0 | |a Transition Metals in Catalysis : |b The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
300 | |a 1 online resource (186 pages). | ||
336 | |a text |b txt |2 rdacontent | ||
337 | |a computer |b c |2 rdamedia | ||
338 | |a online resource |b cr |2 rdacarrier | ||
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540 | |a Creative Commons |f https://creativecommons.org/licenses/by/4.0/ |2 cc |4 https://creativecommons.org/licenses/by/4.0/ | ||
546 | |a English | ||
650 | 7 | |a Research & information: general |2 bicssc | |
650 | 7 | |a Biology, life sciences |2 bicssc | |
653 | |a CO dehydrogenase | ||
653 | |a dihydrogen | ||
653 | |a hydrogenase | ||
653 | |a quantum/classical modeling | ||
653 | |a density functional theory | ||
653 | |a metal-dithiolene | ||
653 | |a pyranopterin molybdenum enzymes | ||
653 | |a fold-angle | ||
653 | |a tungsten enzymes | ||
653 | |a electronic structure | ||
653 | |a pseudo-Jahn-Teller effect | ||
653 | |a thione | ||
653 | |a molybdenum cofactor | ||
653 | |a Moco | ||
653 | |a mixed-valence complex | ||
653 | |a dithiolene ligand | ||
653 | |a tetra-nuclear nickel complex | ||
653 | |a X-ray structure | ||
653 | |a magnetic moment | ||
653 | |a formate hydrogenlyase | ||
653 | |a hydrogen metabolism | ||
653 | |a energy conservation | ||
653 | |a MRP (multiple resistance and pH)-type Na+/H+ antiporter | ||
653 | |a CCCP-carbonyl cyanide m-chlorophenyl-hydrazone | ||
653 | |a EIPA-5-(N-ethyl-N-isopropyl)-amiloride | ||
653 | |a nicotinamide adenine dinucleotide (NADH) | ||
653 | |a electron transfer | ||
653 | |a enzyme kinetics | ||
653 | |a enzyme structure | ||
653 | |a formate dehydrogenase | ||
653 | |a carbon assimilation | ||
653 | |a Moco biosynthesis | ||
653 | |a Fe-S cluster assembly | ||
653 | |a l-cysteine desulfurase | ||
653 | |a ISC | ||
653 | |a SUF | ||
653 | |a NIF | ||
653 | |a iron | ||
653 | |a molybdenum | ||
653 | |a sulfur | ||
653 | |a tungsten cofactor | ||
653 | |a aldehyde:ferredoxin oxidoreductase | ||
653 | |a benzoyl-CoA reductase | ||
653 | |a acetylene hydratase | ||
653 | |a [Fe]-hydrogenase | ||
653 | |a FeGP cofactor | ||
653 | |a guanylylpyridinol | ||
653 | |a conformational changes | ||
653 | |a X-ray crystallography | ||
653 | |a iron-sulfur cluster | ||
653 | |a persulfide | ||
653 | |a metallocofactor | ||
653 | |a frataxin | ||
653 | |a Friedreich's ataxia | ||
653 | |a n/a | ||
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856 | 4 | 0 | |a www.oapen.org |u https://directory.doabooks.org/handle/20.500.12854/68459 |7 0 |z DOAB: description of the publication |
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