Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Catalytic reduction of CN-, CO, and CO2 by nitrogenase cofactors in lanthanide-driven reactions.

ABSTRACT: Nitrogenase cofactors can be extracted into an organic solvent to catalyze the reduction of cyanide (CN(-)), carbon monoxide (CO), and carbon dioxide (CO2) without using adenosine triphosphate (ATP), when samarium(II) iodide (SmI2) and 2,6-lutidinium triflate (Lut-H) are employed as a reductant and a proton source, respectively. Driven by SmI2, the cofactors catalytically reduce CN(-) or CO to C1-C4 hydrocarbons, and CO2 to CO and C1-C3 hydrocarbons. The C-C coupling from CO2 indicates a unique Fischer-Tropsch-like reaction with an atypical carbonaceous substrate, whereas the catalytic turnover of CN(-), CO, and CO2 by isolated cofactors suggests the possibility to develop nitrogenase-based electrocatalysts for the production of hydrocarbons from these carbon-containing compounds.

SUBMITTER: Lee CC

PROVIDER: S-EPMC4300254 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Catalytic reduction of CN-, CO, and CO2 by nitrogenase cofactors in lanthanide-driven reactions.

Lee Chi Chung CC Hu Yilin Y Ribbe Markus W MW

Angewandte Chemie (International ed. in English) 20141124 4

Nitrogenase cofactors can be extracted into an organic solvent to catalyze the reduction of cyanide (CN(-)), carbon monoxide (CO), and carbon dioxide (CO2) without using adenosine triphosphate (ATP), when samarium(II) iodide (SmI2) and 2,6-lutidinium triflate (Lut-H) are employed as a reductant and a proton source, respectively. Driven by SmI2, the cofactors catalytically reduce CN(-) or CO to C1-C4 hydrocarbons, and CO2 to CO and C1-C3 hydrocarbons. The C-C coupling from CO2 indicates a unique ...[more]

PMID: 25420957

Similar Datasets

Biosynthesis of Nitrogenase Cofactors.

Project description:Nitrogenase harbors three distinct metal prosthetic groups that are required for its activity. The simplest one is a [4Fe-4S] cluster located at the Fe protein nitrogenase component. The MoFe protein component carries an [8Fe-7S] group called P-cluster and a [7Fe-9S-C-Mo-R-homocitrate] group called FeMo-co. Formation of nitrogenase metalloclusters requires the participation of the structural nitrogenase components and many accessory proteins, and occurs both in situ, for the P-cluster, and in external assembly sites for FeMo-co. The biosynthesis of FeMo-co is performed stepwise and involves molecular scaffolds, metallochaperones, radical chemistry, and novel and unique biosynthetic intermediates. This review provides a critical overview of discoveries on nitrogenase cofactor structure, function, and activity over the last four decades.

| S-EPMC7318056 | biostudies-literature

CO2 Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane.

Project description:The reduction of N2 to NH3 by Mo-dependent nitrogenase at its active-site metal cluster FeMo-cofactor utilizes reductive elimination of Fe-bound hydrides with obligatory loss of H2 to activate the enzyme for binding/reduction of N2. Earlier work showed that wild-type nitrogenase and a nitrogenase with amino acid substitutions in the MoFe protein near FeMo-cofactor can catalytically reduce CO2 by two or eight electrons/protons to carbon monoxide (CO) and methane (CH4) at low rates. Here, it is demonstrated that nitrogenase preferentially reduces CO2 by two electrons/protons to formate (HCOO(-)) at rates >10 times higher than rates of CO2 reduction to CO and CH4. Quantum mechanical calculations on the doubly reduced FeMo-cofactor with a Fe-bound hydride and S-bound proton (E2(2H) state) favor a direct reaction of CO2 with the hydride ("direct hydride transfer" reaction pathway), with facile hydride transfer to CO2 yielding formate. In contrast, a significant barrier is observed for reaction of Fe-bound CO2 with the hydride ("associative" reaction pathway), which leads to CO and CH4. Remarkably, in the direct hydride transfer pathway, the Fe-H behaves as a hydridic hydrogen, whereas in the associative pathway it acts as a protic hydrogen. MoFe proteins with amino acid substitutions near FeMo-cofactor (?-70(Val?Ala), ?-195(His?Gln)) are found to significantly alter the distribution of products between formate and CO/CH4.

| S-EPMC5068488 | biostudies-literature

Catalytic CO2 Reduction with Boron- and Aluminum Hydrides.

Project description:The previously reported dimeric NHI aluminum dihydrides 1 a,b, as well as the bis(NHI) aluminum dihydride salt 9 +[OTs]-, the bis(NHI) boron dihydride salt 10 +[OTs]-, and the "free" bis(NHI) ligand 12 were investigated with regard to their activity as a homogenous (pre)catalyst in the hydroboration (i. e. catalytic reduction) of carbon dioxide (CO2) in chloroform under mild conditions (i. e. room temperature, 1 atm; NHI=N-heterocyclic imine, Ts=tosyl). Borane dimethylsulfide complex and catecholborane were used as a hydride source. Surprisingly, the less sterically hindered 1 a exhibited lower catalytic activity than the bulkier 1 b. A similarly unexpected discrepancy was found with the lower catalytic activity of 10 + in comparison to the one of the bis(NHI) 12. The latter is incorporated as the ligand to the boron center in 10 +. To elucidate possible mechanisms for CO2 reduction the compounds were subjected to stoichiometric reactivity studies with the borane or CO2. Aluminum carboxylates 4, 6, and 7 + with two, four, and one formate group per two aluminum centers were isolated. Also, the boron formate salt 11 +[OTs]- was characterized. Selected metal formates were subjected to stoichiometric reactions with boranes and/or tested as a catalyst. We conclude that each type of catalyst (1 a,b, 9 +, 10 +, 12) follows an individual mechanistic pathway for CO2 reduction.

| S-EPMC6919925 | biostudies-literature

Catalytic Activity of Thermolyzed [Co(NH3)6][Fe(CN)6] in CO Hydrogenation Reaction.

Project description:Currently, the processes of obtaining synthetic liquid hydrocarbons and oxygenates are very relevant. Fischer-Tropsch synthesis (FTS) is the most important step in these processes. The products of thermal destruction in argon of the mixture [Co(NH3)6][Fe(CN)6] and Al(OH)3 were used as catalysts for CO hydrogenation. The resulting compositions were studied using powder X-ray diffraction, IR spectroscopy, elemental analysis, SEM micrographs. The specific surface area, pore and particle size distributions were determined. It was determined that the DCS-based catalysts were active in the high-temperature Fischer-Tropsch synthesis. The effect of aluminum in the catalyst composition on the distribution of reaction products was revealed.

| S-EPMC8270307 | biostudies-literature

Electrocatalytic and Solar-Driven CO2 Reduction to CO with a Molecular Manganese Catalyst Immobilized on Mesoporous TiO2.

Project description:Electrocatalytic CO2 reduction to CO was achieved with a novel Mn complex, fac-[MnBr(4,4'-bis(phosphonic acid)-2,2'-bipyridine)(CO)3 ] (MnP), immobilized on a mesoporous TiO2 electrode. A benchmark turnover number of 112±17 was attained with these TiO2 |MnP electrodes after 2?h electrolysis. Post-catalysis IR spectroscopy demonstrated that the molecular structure of the MnP catalyst was retained. UV/vis spectroscopy confirmed that an active Mn-Mn dimer was formed during catalysis on the TiO2 electrode, showing the dynamic formation of a catalytically active dimer on an electrode surface. Finally, we combined the light-protected TiO2 |MnP cathode with a CdS-sensitized photoanode to enable solar-light-driven CO2 reduction with the light-sensitive MnP catalyst.

| S-EPMC5074277 | biostudies-literature

Data on the catalytic CO oxidation and CO2 reduction durability on gC3N4 nanotubes Co-doped atomically with Pd and Cu.

Project description:Understanding the fabrication mechanism of graphitic carbon nitride (gC3N4) nanostructures is critical for tailoring their physicochemical properties for various catalytic applications. In this article, we provide deep insights into the optimized parameters for the rational synthesis of one-dimensional gC3N4 atomically doped with Pd and Cu denoted as (Pd/Cu/gC3N4NTs) and its fabrication mechanism. This is in addition to the CO oxidation durability along with the electrochemical and photoelectrochemical CO2 reduction durability of Pd/Cu/gC3N4NTs. The presented herein results are correlated to the research article entitled "Precise Fabrication of Porous One-dimensional gC3N4 Nanotubes Doped with Pd and Cu Atoms for Efficient CO Oxidation and CO2 Reduction (Kamel Eid et al., 2019).

| S-EPMC6811889 | biostudies-other

Lanthanide ions as required cofactors for DNA catalysts.

Project description:We report that micromolar concentrations of lanthanide ions can be required cofactors for DNA-hydrolyzing deoxyribozymes. Previous work identified deoxyribozymes that simultaneously require both Zn(2+) and Mn(2+) to achieve DNA-catalyzed DNA hydrolysis (10(12) rate enhancement); a mutant of one such DNA catalyst requires only Zn(2+). Here we show that in vitro selection in the presence of 10 µM lanthanide ion (Ce(3+), Eu(3+), or Yb(3+)) along with 1 mM Zn(2+) leads to numerous DNA-hydrolyzing deoxyribozymes that strictly require the lanthanide ion as well as Zn(2+) for catalytic activity. These DNA catalysts have a range of lanthanide dependences, including some deoxyribozymes that strongly favor one particular lanthanide ion (e.g., Ce(3+) >> Eu(3+) >> Yb(3+)) and others that function well with more than one lanthanide ion. Intriguingly, two of the Yb(3+)-dependent deoxyribozymes function well with Yb(3+) alone (K(d,app) ~10 µM, in the absence of Zn(2+)) and have little or no activity with Eu(3+) or Ce(3+). In contrast to these selection outcomes when lanthanide ions were present, new selections with Zn(2+) or Mn(2+) alone, or Zn(2+) with Mg(2+)/Ca(2+), led primarily to deoxyribozymes that cleave DNA by deglycosylation and ?-elimination rather than by hydrolysis, including several instances of depyrimidination. We conclude that lanthanide ions warrant closer attention as cofactors when identifying new nucleic acid catalysts, especially for applications in which high concentrations of polyvalent metal ion cofactors are undesirable.

| S-EPMC3521562 | biostudies-literature

Visible light-driven CO2 reduction by enzyme coupled CdS nanocrystals.

Project description:Assemblies of carbon monoxide dehydrogenase molecules with CdS nanocrystals show fast CO(2) reduction driven by visible light. Activity is strongly influenced by size and shape of nanocrystals, and by the nature of the electron donor.

| S-EPMC3553213 | biostudies-literature

Evaluation of the Catalytic Relevance of the CO-Bound States of V-Nitrogenase.

Project description:Binding and activation of CO by nitrogenase is a topic of interest because CO is isoelectronic to N2 , the physiological substrate of this enzyme. The catalytic relevance of one- and multi-CO-bound states (the lo-CO and hi-CO states) of V-nitrogenase to C-C coupling and N2 reduction was examined. Enzymatic and spectroscopic studies demonstrate that the multiple CO moieties in the hi-CO state cannot be coupled as they are, suggesting that C-C coupling requires further activation and/or reduction of the bound CO entity. Moreover, these studies reveal an interesting correlation between decreased activity of N2 reduction and increased population of the lo-CO state, pointing to the catalytic relevance of the belt Fe atoms that are bridged by the single CO moiety in the lo-CO state. Together, these results provide a useful framework for gaining insights into the nitrogenase-catalyzed reaction via further exploration of the utility of the lo-CO conformation of V-nitrogenase.

| S-EPMC6364567 | biostudies-literature

An internal electron reservoir enhances catalytic CO2 reduction by a semisynthetic enzyme.

Project description:The development of an artificial metalloenzyme for CO2 reduction is described. The small-molecule catalyst [Ni(II)(cyclam)](2+) has been incorporated within azurin. Selectivity for CO generation over H(+) reduction is enhanced within the protein environment, while the azurin active site metal impacts the electrochemical overpotential and photocatalytic activity. The enhanced catalysis observed for copper azurin suggests an important role for intramolecular electron transfer, analogous to native CO2 reducing enzymes.

| S-EPMC4977188 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data