caa a22 4500 605507791 CHVBK 20210128100633.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1218-2 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1218-2 Molybdenum and tungsten-dependent formate dehydrogenases [Elektronische Daten] [Luisa Maia, José Moura, Isabel Moura] 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. SBIC, 2014 Molybdenum nationallicence Tungsten nationallicence Formate oxidation nationallicence Carbon dioxide reduction nationallicence Formate-dependent energy metabolism nationallicence Sulfur-shift nationallicence DMSOR : Dimethylsulfoxide reductase nationallicence EPR : Electron paramagnetic resonance spectroscopy nationallicence FDH : Formate dehydrogenase nationallicence FDH-H : E. coli formate dehydrogenase H, from the formate-hydrogen lyase system nationallicence FDH-N : E. coli formate dehydrogenase N, from the anaerobic nitrate-formate respiratory pathway nationallicence FDH-O : E. coli formate dehydrogenase O, from the aerobic respiratory pathways nationallicence Fe/S : Iron-sulfur centre nationallicence Mo-FDH : Molybdenum-dependent formate dehydrogenase nationallicence Mo/W-FDH : Formate dehydrogenase that incorporates either molybdenum or tungsten nationallicence Mo/NAD-FDH : Molybdenum-dependent/NAD-dependent formate dehydrogenase nationallicence Mo/W-bis PGD : Molybdenum/tungsten-bis pyranopterin guanosine dinucleotide-containing enzymes nationallicence NAD-FDH : NAD-dependent formate dehydrogenase nationallicence NarGHI : Respiratory nitrate reductase, after the name of the encoding genes, narG, H, and I nationallicence PGD : Pyranopterin guanosine dinucleotide cofactor nationallicence W/NAD-FDH : Tungsten-dependent/NAD-dependent formate dehydrogenase nationallicence W-FDH : Tungsten-dependent formate dehydrogenase nationallicence Maia Luisa UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut Moura José UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut Moura Isabel UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 287-309 0949-8257 20:2<287 2015 20 775 https://doi.org/10.1007/s00775-014-1218-2 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1218-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Maia Luisa UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut NATIONALLICENCE 700 1- Moura José UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut NATIONALLICENCE 700 1- Moura Isabel UCIBIO@REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 287-309 0949-8257 20:2<287 2015 20 775