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Formate production through biocatalysis

dc.contributor.authorAlissandratos, Lee
dc.contributor.authorKim, Hye-Kyung
dc.contributor.authorEaston, Christopher
dc.date.accessioned2015-12-10T23:04:35Z
dc.date.issued2013
dc.date.updated2020-07-05T08:18:06Z
dc.description.abstractThe generation of formate from CO2 provides a method for sequestration of this greenhouse gas as well as the production of a valuable commodity chemical and stabilized form of hydrogen fuel. Formate dehydrogenases are enzymes with the potential to catalyze this reaction; however they generally favor the reverse process, i.e., formate oxidation. By contrast, the formate dehydrogenase of the acetogen Clostridium carboxidivorans has been found to preferentially catalyze the reduction of CO2. This is in accord with its natural role to introduce CO2 as a carbon source in the Wood-Ljungdahl pathway. The direction of catalysis derives from the enzyme's low affinity for formate. This enzyme is therefore an excellent candidate for biotechnological applications aimed at producing formic acid and derivative chemicals from CO2.
dc.identifier.issn1949-1026
dc.identifier.urihttp://hdl.handle.net/1885/62431
dc.publisherLandes Bioscience
dc.sourceBioengineered
dc.subjectKeywords: bacterial protein; carbon dioxide; formate dehydrogenase; formic acid; formic acid derivative; acetogens; article; biocatalysis; carbon cycle; Clostridium; Clostridium carboxidivorans; CO2 fixation; CO2 reduction; enzymology; genetics; Hydrogen storage; k
dc.titleFormate production through biocatalysis
dc.typeJournal article
local.bibliographicCitation.issue5
local.bibliographicCitation.lastpage350
local.bibliographicCitation.startpage348
local.contributor.affiliationAlissandratos, Lee, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationKim, Hye-Kyung, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationEaston, Christopher, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidAlissandratos, Lee, u5109855
local.contributor.authoruidKim, Hye-Kyung, u4025060
local.contributor.authoruidEaston, Christopher, u9500570
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030401 - Biologically Active Molecules
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciences
local.identifier.ariespublicationu4005981xPUB698
local.identifier.citationvolume4
local.identifier.doi10.4161/bioe.25360
local.identifier.scopusID2-s2.0-84898184406
local.identifier.thomsonID000336904300017
local.type.statusPublished Version

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