ArticleBiochemistry2014
Solvent isotope effects on alkane formation by cyanobacterial aldehyde deformylating oxygenase and their mechanistic implications.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Insights into cyanobacterial alkane biosynthesis.Journal of industrial microbiology & biotechnology · 2022Review
- Addition of formate dehydrogenase increases the production of renewable alkane from an engineered metabolic pathway.The Journal of biological chemistry · 2019Article
- A consensus-guided approach yields a heat-stable alkane-producing enzyme and identifies residues promoting thermostability.The Journal of biological chemistry · 2018Article
- Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship.BMC biotechnology · 2017Article
- Structure-oriented substrate specificity engineering of aldehyde-deformylating oxygenase towards aldehydes carbon chain length.Biotechnology for biofuels · 2016Article
- Conversion of Aldehyde to Alkane by a Peroxoiron(III) Complex: A Functional Model for the Cyanobacterial Aldehyde-Deformylating Oxygenase.Journal of the American Chemical Society · 2015Article
- Chemoselective formation of unsymmetrically substituted ethers from catalytic reductive coupling of aldehydes and ketones with alcohols in aqueous solution.Organic letters · 2015Article
- Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound.ACS chemical biology · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The reaction catalyzed by cyanobacterial aldehyde deformylating oxygenase is of interest both because of its potential application to the production of biofuels and because of the highly unusual nature of the deformylation reaction it catalyzes. Whereas the proton in the product alkane derives ultimately from the solvent, the identity of the proton donor in the active site remains unclear. To investigate the proton transfer step, solvent isotope effect (SIE) studies were undertaken. The rate of alkane formation was found to be maximal at pH 6.8 and to be the same in D2O or H2O within experimental error, implying that proton transfer is not a kinetically significant step. However, when the ratio of protium to deuterium in the product alkane was measured as a function of the mole fraction of D2O, a (D2O)SIEobs of 2.19 ± 0.02 was observed. The SIE was invariant with the mole fraction of D2O, indicating the involvement of a single protic site in the reaction. We interpret this SIE as most likely arising from a reactant state equilibrium isotope effect on a proton donor with an inverse fractionation factor, for which Φ = 0.45. These observations are consistent with an iron-bound water molecule being the proton donor to the alkane in the reaction.
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