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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Schwanhold, Nadine Hartmann, Tobias Leimkühler, Silke |
| Description | Author Affiliation: Hartmann T ( Institute of Biochemistry and Biology, Department of Molecular Enzymology, University of Potsdam, D-14476 Potsdam, Germany.); Schwanhold N ( Institute of Biochemistry and Biology, Department of Molecular Enzymology, University of Potsdam, D-14476 Potsdam, Germany.); Leimkühler S ( Institute of Biochemistry and Biology, Department of Molecular Enzymology, University of Potsdam, D-14476 Potsdam, Germany. Electronic address: sleim@uni-potsdam.de.) |
| Abstract | The global carbon cycle depends on the biological transformations of C $_{1}$ compounds, which include the reductive incorporation of CO $_{2}$ into organic molecules (e.g. in photosynthesis and other autotrophic pathways), in addition to the production of CO $_{2}$ from formate, a reaction that is catalyzed by formate dehydrogenases (FDHs). FDHs catalyze, in general, the oxidation of formate to CO $_{2}$ and H $^{+}$ . However, selected enzymes were identified to act as CO $_{2}$ reductases, which are able to reduce CO $_{2}$ to formate under physiological conditions. This reaction is of interest for the generation of formate as a convenient storage form of H $_{2}$ for future applications. Cofactor-containing FDHs are found in anaerobic bacteria and archaea, in addition to facultative anaerobic or aerobic bacteria. These enzymes are highly diverse and employ different cofactors such as the molybdenum cofactor (Moco), FeS clusters and flavins, or cytochromes. Some enzymes include tungsten (W) in place of molybdenum (Mo) at the active site. For catalytic activity, a selenocysteine (SeCys) or cysteine (Cys) ligand at the Mo atom in the active site is essential for the reaction. This review will focus on the characterization of Mo- and W-containing FDHs from bacteria, their active site structure, subunit compositions and its proposed catalytic mechanism. We will give an overview on the different mechanisms of substrate conversion available so far, in addition to providing an outlook on bio-applications of FDHs. This article is part of a Special Issue entitled: Cofactor-dependent proteins: evolution, chemical diversity and bio-applications. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 9 |
| Volume Number | 1854 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-09-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Bacteria Enzymology Formate Dehydrogenases Chemistry Molybdenum Tungsten Catalysis Catalytic Domain Metabolism Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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