Molybdenum and tungsten-dependent formate dehydrogenases
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| 024 | 7 | 0 | |a 10.1007/s00775-014-1218-2 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-014-1218-2 | ||
| 245 | 0 | 0 | |a Molybdenum and tungsten-dependent formate dehydrogenases |h [Elektronische Daten] |c [Luisa Maia, José Moura, Isabel Moura] |
| 520 | 3 | |a The prokaryotic formate metabolism is considerably diversified. Prokaryotes use formate in the C1 metabolism, but also evolved to exploit the low reduction potential of formate to derive energy, by coupling its oxidation to the reduction of numerous electron acceptors. To fulfil these varied physiological roles, different types of formate dehydrogenase (FDH) enzymes have evolved to catalyse the reversible 2-electron oxidation of formate to carbon dioxide. This review will highlight our present knowledge about the diverse physiological roles of FDH in prokaryotes, their modular structural organisation and active site structures and the mechanistic strategies followed to accomplish the formate oxidation. In addition, the ability of FDH to catalyse the reverse reaction of carbon dioxide reduction, a potentially relevant reaction for carbon dioxide sequestration, will also be addressed. | |
| 540 | |a SBIC, 2014 | ||
| 690 | 7 | |a Molybdenum |2 nationallicence | |
| 690 | 7 | |a Tungsten |2 nationallicence | |
| 690 | 7 | |a Formate oxidation |2 nationallicence | |
| 690 | 7 | |a Carbon dioxide reduction |2 nationallicence | |
| 690 | 7 | |a Formate-dependent energy metabolism |2 nationallicence | |
| 690 | 7 | |a Sulfur-shift |2 nationallicence | |
| 690 | 7 | |a DMSOR : Dimethylsulfoxide reductase |2 nationallicence | |
| 690 | 7 | |a EPR : Electron paramagnetic resonance spectroscopy |2 nationallicence | |
| 690 | 7 | |a FDH : Formate dehydrogenase |2 nationallicence | |
| 690 | 7 | |a FDH-H : E. coli formate dehydrogenase H, from the formate-hydrogen lyase system |2 nationallicence | |
| 690 | 7 | |a FDH-N : E. coli formate dehydrogenase N, from the anaerobic nitrate-formate respiratory pathway |2 nationallicence | |
| 690 | 7 | |a FDH-O : E. coli formate dehydrogenase O, from the aerobic respiratory pathways |2 nationallicence | |
| 690 | 7 | |a Fe/S : Iron-sulfur centre |2 nationallicence | |
| 690 | 7 | |a Mo-FDH : Molybdenum-dependent formate dehydrogenase |2 nationallicence | |
| 690 | 7 | |a Mo/W-FDH : Formate dehydrogenase that incorporates either molybdenum or tungsten |2 nationallicence | |
| 690 | 7 | |a Mo/NAD-FDH : Molybdenum-dependent/NAD-dependent formate dehydrogenase |2 nationallicence | |
| 690 | 7 | |a Mo/W-bis PGD : Molybdenum/tungsten-bis pyranopterin guanosine dinucleotide-containing enzymes |2 nationallicence | |
| 690 | 7 | |a NAD-FDH : NAD-dependent formate dehydrogenase |2 nationallicence | |
| 690 | 7 | |a NarGHI : Respiratory nitrate reductase, after the name of the encoding genes, narG, H, and I |2 nationallicence | |
| 690 | 7 | |a PGD : Pyranopterin guanosine dinucleotide cofactor |2 nationallicence | |
| 690 | 7 | |a W/NAD-FDH : Tungsten-dependent/NAD-dependent formate dehydrogenase |2 nationallicence | |
| 690 | 7 | |a W-FDH : Tungsten-dependent formate dehydrogenase |2 nationallicence | |
| 700 | 1 | |a Maia |D Luisa |u UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | |
| 700 | 1 | |a Moura |D José |u UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | |
| 700 | 1 | |a Moura |D Isabel |u UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 287-309 |x 0949-8257 |q 20:2<287 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1218-2 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a review-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-014-1218-2 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Maia |D Luisa |u UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Moura |D José |u UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Moura |D Isabel |u UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 287-309 |x 0949-8257 |q 20:2<287 |1 2015 |2 20 |o 775 | ||