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      Formate Formation and Formate Conversion in Biological Fuels Production

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          Abstract

          Biomethanation is a mature technology for fuel production. Fourth generation biofuels research will focus on sequestering CO 2 and providing carbon-neutral or carbon-negative strategies to cope with dwindling fossil fuel supplies and environmental impact. Formate is an important intermediate in the methanogenic breakdown of complex organic material and serves as an important precursor for biological fuels production in the form of methane, hydrogen, and potentially methanol. Formate is produced by either CoA-dependent cleavage of pyruvate or enzymatic reduction of CO 2 in an NADH- or ferredoxin-dependent manner. Formate is consumed through oxidation to CO 2 and H 2 or can be further reduced via the Wood-Ljungdahl pathway for carbon fixation or industrially for the production of methanol. Here, we review the enzymes involved in the interconversion of formate and discuss potential applications for biofuels production.

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            Methanogenic archaea: ecologically relevant differences in energy conservation.

            Rudolf Thauer, Anne-Kristin Kaster, Henning Seedorf … (2008)
            Most methanogenic archaea can reduce CO(2) with H(2) to methane, and it is generally assumed that the reactions and mechanisms of energy conservation that are involved are largely the same in all methanogens. However, this does not take into account the fact that methanogens with cytochromes have considerably higher growth yields and threshold concentrations for H(2) than methanogens without cytochromes. These and other differences can be explained by the proposal outlined in this Review that in methanogens with cytochromes, the first and last steps in methanogenesis from CO(2) are coupled chemiosmotically, whereas in methanogens without cytochromes, these steps are energetically coupled by a cytoplasmic enzyme complex that mediates flavin-based electron bifurcation.
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              Reversible interconversion of carbon dioxide and formate by an electroactive enzyme.

              Judy Hirst, Torsten Reda, Caroline Plugge … (2008)
              Carbon dioxide (CO(2)) is a kinetically and thermodynamically stable molecule. It is easily formed by the oxidation of organic molecules, during combustion or respiration, but is difficult to reduce. The production of reduced carbon compounds from CO(2) is an attractive proposition, because carbon-neutral energy sources could be used to generate fuel resources and sequester CO(2) from the atmosphere. However, available methods for the electrochemical reduction of CO(2) require excessive overpotentials (are energetically wasteful) and produce mixtures of products. Here, we show that a tungsten-containing formate dehydrogenase enzyme (FDH1) adsorbed to an electrode surface catalyzes the efficient electrochemical reduction of CO(2) to formate. Electrocatalysis by FDH1 is thermodynamically reversible--only small overpotentials are required, and the point of zero net catalytic current defines the reduction potential. It occurs under thoroughly mild conditions, and formate is the only product. Both as a homogeneous catalyst and on the electrode, FDH1 catalyzes CO(2) reduction with a rate more than two orders of magnitude faster than that of any known catalyst for the same reaction. Formate oxidation is more than five times faster than CO(2) reduction. Thermodynamically, formate and hydrogen are oxidized at similar potentials, so formate is a viable energy source in its own right as well as an industrially important feedstock and a stable intermediate in the conversion of CO(2) to methanol and methane. FDH1 demonstrates the feasibility of interconverting CO(2) and formate electrochemically, and it is a template for the development of robust synthetic catalysts suitable for practical applications.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Enzyme Res
                Journal ID (publisher-id): ER
                Title: Enzyme Research
                Publisher: SAGE-Hindawi Access to Research
                ISSN (Electronic): 2090-0414
                Publication date Collection: 2011
                Publication date (Electronic): 24 May 2011
                Volume: 2011
                Electronic Location Identifier: 532536
                Affiliations
                1Department of Botany and Microbiology, University of Oklahoma, Norman, OK 73019, USA
                2Laboratorium voor Microbiologie, Wageningen Universiteit, Dreijenplein 10, 6703 HB Wageningen, The Netherlands
                Author notes
                *Alfons J. M. Stams: fons.stams@ 123456wur.nl

                Academic Editor: Subramanian Ramakrishnan

                Article
                DOI: 10.4061/2011/532536
                PMC ID: 3112519
                PubMed ID: 21687599
                SO-VID: 5af0aa28-874e-4474-9d7a-bda3b0c6269f
                Copyright © Copyright © 2011 Bryan R. Crable et al.
                License:

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 15 January 2011
                Date accepted : 23 March 2011
                Categories
                Subject: Review Article

                ScienceOpen disciplines: Biochemistry
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                ScienceOpen disciplines: Biochemistry

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