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Cupriavidus necator

January 01, 1970

Cupriavidus necator is a Gram-negative soil bacterium of the class Betaproteobacteria.[1]

Cupriavidus necator
Scientific classification
Domain:
Bacteria
Phylum:
Pseudomonadota
Class:
Betaproteobacteria
Order:
Burkholderiales
Family:
Burkholderiaceae
Genus:
Cupriavidus
Species:
C. necator
Binomial name
Cupriavidus necator
(Davis 1969) Yabuuchi et al. 1996
Synonyms

Ralstonia eutropha

Taxonomy edit

Cupriavidus necator has gone through a series of name changes. In the first half of the 20th century, many micro-organisms were isolated for their ability to use hydrogen. Hydrogen-metabolizing chemolithotrophic organisms were clustered into the group Hydrogenomonas.[2] C. necator was originally named Hydrogenomonas eutrophus because it fell under the Hydrogenomonas classification and was "well nourished and robust".[3] Some of the original H. eutrophus cultures isolated were by Bovell and Wilde.[4][5] After characterizing cell morphology, metabolism and GC content, the Hydrogenomonas nomenclature was disbanded because it comprised many species of microorganisms.[2] H. eutrophus was then renamed Alcaligenes eutropha because it was a micro-organism with degenerated peritrichous flagellation.[3][6] Investigating phenotype, lipid composition, fatty acid composition and 16S rRNA analysis, A. eutropha was found to belong to the genus Ralstonia and named Ralstonia eutropha.[1] Upon further study of the genus, Ralstonia was found to comprise two phenotypically distinct clusters. The new genus Wautersia was created from one of these clusters which included R. eutropha. In turn R. eutropha was renamed Wautersia eutropha.[7] Looking at DNA–DNA hybridization and phenotype comparison with Cupriavidus necator, W. eutropha was found to be the same species as previously described C. necator. Because C. necator was named in 1987 far before the name change to R. eutropha and W. eutropha, the name C. necator was assigned to R. eutropha according to Rule 23a of the International Code of Nomenclature of Bacteria.[8]

Metabolism edit

Cupriavidus necator is a hydrogen-oxidizing bacterium ("knallgas" bacterium) capable of growing at the interface of anaerobic and aerobic environments. It can easily adapt between heterotrophic and autotrophic lifestyles. Both organic compounds and hydrogen can be used as a source of energy[9] C. necator can perform aerobic or anaerobic respiration by denitrification of nitrate and/or nitrite to nitrogen gas.[10] When growing under autotrophic conditions, C. necator fixes carbon through the reductive pentose phosphate pathway.[11] It is known to produce and sequester polyhydroxyalkanoate (PHA) plastics when exposed to excess amounts of sugar substrate. PHA can accumulate to levels around 90% of the cell's dry weight.[12] To better characterize the lifestyle of C. necator, the genomes of two strains have been sequenced.[9][13]

Hydrogenases edit

Cupriavidus necator can use hydrogen gas as a source of energy when growing under autotrophic conditions. It contains four different hydrogenases that have [Ni-Fe] active sites and all perform this reaction:[14][15]

H2   2H+ + 2e−

The hydrogenases of C. necator are like other typical [Ni-Fe] hydrogenases because they are made up of a large and a small subunit. The large subunit is where the [Ni-Fe] active site resides and the small subunit is composed of [Fe-S] clusters.[16] However, the hydrogenases of C. necator are different from typical [Ni-Fe] hydrogenases because they are tolerant to oxygen and are not inhibited by CO.[14] While the four hydrogenases perform the same reaction in the cell, each hydrogenase is linked to a different cellular process. The differences between the regulatory hydrogenase, membrane-bound hydrogenase, soluble hydrogenase and actinobacterial hydrogenase in C. necator are described below.

Regulatory hydrogenase edit

The first hydrogenase is a regulatory hydrogenase (RH) that signals to the cell hydrogen is present. The RH is a protein containing large and small [Ni-Fe] hydrogenase subunits attached to a histidine protein kinase subunit.[17] The hydrogen gas is oxidized at the [Ni-Fe] center in the large subunit and in turn reduces the [Fe-S] clusters in the small subunit. It is unknown whether the electrons are transferred from the [Fe-S] clusters to the protein kinase domain.[14] The histidine protein kinase activates a response regulator. The response regulator is active in the dephosphorylated form. The dephosphorylated response regulator promotes the transcription of the membrane bound hydrogenase and soluble hydrogenase.[18]

Membrane-bound hydrogenase edit

The membrane-bound hydrogenase (MBH) is linked to the respiratory chain through a specific cytochrome b-related protein in C. necator.[19] Hydrogen gas is oxidized at the [Ni-Fe] active site in the large subunit and the electrons are shuttled through the [Fe-S] clusters in the small subunit to the cytochrome b-like protein.[14] The MBH is located on the outer cytoplasmic membrane. It recovers energy for the cell by funneling electrons into the respiratory chain and by increasing the proton gradient.[19] The MBH in C. necator is not inhibited by CO and is tolerant to oxygen.[20]

NAD+-reducing hydrogenase edit

The NAD+-reducing hydrogenase (soluble hydrogenase, SH) creates a NADH-reducing equivalence by oxidizing hydrogen gas. The SH is a heterohexameric protein[21] with two subunits making up the large and small subunits of the [Ni-Fe] hydrogenase and the other two subunits comprising a reductase module similar to the one of Complex I.[22] The [Ni-Fe] active site oxidized hydrogen gas which transfers electrons to a FMN-a cofactor, then to a [Fe-S] cluster relay of the small hydrogenase subunit and the reductase module, then to another FMN-b cofactor and finally to NAD+.[14] The reducing equivalences are then used for fixing carbon dioxide when C. necator is growing autotrophically.

The active site of the SH of C. necator H16 has been extensively studied because C. necator H16 can be produced in large amounts, can be genetically manipulated, and can be analyzed with spectrographic techniques. However, no crystal structure is currently available for the C. necator H16 soluble hydrogenase in the presence of oxygen to determine the interactions of the active site with the rest of the protein.[14]

Typical anaerobic [Ni-Fe] hydrogenases edit

The [Ni-Fe] hydrogenase from Desulfovibrio vulgaris and D. gigas have similar protein structures to each other and represent typical [Ni-Fe] hydrogenases.[14][23][24][25] The large subunit contains the [Ni-Fe] active site buried deep in the core of the protein and the small subunit contains [Fe-S] clusters. The Ni atom is coordinated to the Desulfovibrio hydrogenase by 4 cysteine ligands. Two of these same cysteine ligands also bridge the Fe of the [Ni-Fe] active site.[23][24] The Fe atom also contains three ligands, one CO and two CN that complete the active site.[26] These additional ligands might contribute to the reactivity or help stabilize the Fe atom in the low spin +2 oxidation state.[23] Typical [NiFe] hydrogenases like those of D. vulgaris and D. gigas are poisoned by oxygen because an oxygen atom binds strongly to the NiFe active site.[20]

C. necator oxygen-tolerant SH edit

The SH in C. necator are unique for other organisms because it is oxygen tolerant.[27] The active site of the SH has been studied to learn why this protein is tolerant to oxygen. A recent study showed that oxygen tolerance as implemented in the SH is based on a continuous catalytically driven detoxification of O2 [Ref missing].  The genes encoding this SH can be up-regulated under heterotrophic growth condition using glycerol in the growth media [28] and this enables aerobic production and purification of the same enzyme.[29]

Applications edit

The oxygen-tolerant hydrogenases of C. necator have been studied for diverse purposes. C. necator was studied as an attractive organism to help support life in space. It can fix carbon dioxide as a carbon source, use the urea in urine as a nitrogen source, and use hydrogen as an energy source to create dense cultures that could be used as a source of protein.[30][31]

Electrolysis of water is one way of creating oxygenic atmosphere in space and C. necator was investigated to recycle the hydrogen produced during this process.[32]

Oxygen-tolerant hydrogenases are being used to investigate biofuels. Hydrogenases from C. necator have been used to coat electrode surfaces to create hydrogen fuel cells tolerant to oxygen and carbon monoxide[20] and to design hydrogen-producing light complexes.[33] In addition, the hydrogenases from C. necator have been used to create hydrogen sensors.[34] Genetically modified C. necator can produce isobutanol from CO
2 that can directly substitute or blend with gasoline. The organism emits the isobutanol without having to be destroyed to obtain it.[35]

Industrial uses edit

Researchers at UCLA have genetically modified a strain of the species C. necator (formerly known as R. eutropha H16) to produce isobutanol from CO2 feedstock using electricity produced by a solar cell. The project, funded by the U.S. Dept. of Energy, is a potential high energy-density electrofuel that could use existing infrastructure to replace oil as a transportation fuel.[36]

Chemical and biomolecular engineers at Korea Advanced Institute of Science and Technology has presented a scalable way to convert CO2 in the air into a polyester by means of the C. necator.[37]

References edit

  1. ^ a b Yabuuchi; et al. (1995). "Transfer of two Burkholderia and an Alcaligenes species to Ralstonia gen. nov.: proposal of Ralstonia pickettii (Ralston, Palleroni and Doudoroff 1973) comb. nov., Ralstonia solanacearum (Smith 1896) comb. nov. and Ralstonia eutropha (Davis 1969) comb. nov". Microbiol Immunol. 39 (11): 897–904. doi:10.1111/j.1348-0421.1995.tb03275.x. PMID 8657018.
  2. ^ a b Davis, D.; Doudoroff, M. & Stanier, R. (1969). "Proposal to reject the genus Hydrogenomonas: Taxonomic implications". Int J Syst Bacteriol. 19 (4): 375–390. doi:10.1099/00207713-19-4-375.
  3. ^ a b Bowien, B.; Schlegel, H. (1981). "Physiology and biochemistry of aerobic hydrogen-oxidizing bacteria". Annu. Rev. Microbiol. 35: 405–452. doi:10.1146/annurev.mi.35.100181.002201. PMID 6271040.
  4. ^ Repaske, R. (1981). "Nutritional Requirements forHydrogenomonas eutropha". J. Bacteriol. 83 (2): 418–422. doi:10.1128/JB.83.2.418-422.1962. PMC 277745. PMID 14491520.
  5. ^ Wilde, E. (1962). "Untersuchungen über Wachstum und Speicherstoffsynthese von Hydrogenomonas eutropha". Archiv für Mikrobiologie. 43 (2): 109–137. doi:10.1007/bf00406429. S2CID 25824711.
  6. ^ Davis, D.; Stanier, R. & Doudoroff, M. (1970). "Taxonomic Studies on Some Gram Negative Polarly Flagellated "Hydrogen Bacteria" and Related Species". Arch. Mikrobiol. 70 (1): 1–13. doi:10.1007/BF00691056. PMID 4987616. S2CID 24798412.
  7. ^ Vaneechoutte, M.; Kampfer, P.; De Baere, T.; Falsen, E. & Verschraegen, G. (2004). "Wautersia gen. nov., a novel genus accommodating the phylogenetic lineage including Ralstonia eutropha and related species, and proposal of Ralstonia [Pseudomonas] syzygii(Roberts et al. 1990) comb. nov". International Journal of Systematic and Evolutionary Microbiology. 54 (Pt 2): 317–327. doi:10.1099/ijs.0.02754-0. PMID 15023939.
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    2     sensing in Alcaligenes eutrophus". PNAS. 95 (21): 12474–12479. doi:10.1073/pnas.95.21.12474. PMC 22855. PMID 9770510.
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  22. ^ Tran-Betcke, A.; Warnecke, U.; Bocker, C.; Zaborosch, C. & Friedrich, B. (1990). "Cloning and Nucleotide Sequences of the Genes for the Subunits of NAD-Reducing Hydrogenase of Alcaligenes eutrophus H16". Journal of Bacteriology. 172 (6): 2920–2929. doi:10.1128/jb.172.6.2920-2929.1990. PMC 209089. PMID 2188945.
  23. ^ a b c Higuchi, .; Yagi, T. & Yasuoka, N. (1997). "Unusual ligand structure in Ni–Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis". Structure. 5 (12): 1671–1680. doi:10.1016/S0969-2126(97)00313-4. PMID 9438867.
  24. ^ a b Volbeda, A.; Garcin, E.; Piras, C.; de Lacey, A.; Fernandez, V.; Hatchikian, C.; Frey, M. & Fontecilla-Camps, J. (1996). "Structure of the [NiFe] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands". J. Am. Chem. Soc. 118 (51): 12989–12996. doi:10.1021/ja962270g.
  25. ^ Volbeda, A.; Charon, M.; Piras, C.; Hatchikian, C.; Frey, M. & Fontecilla-Camps, J. (1995). "Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas". Nature. 373 (6515): 580–587. doi:10.1038/373580a0. PMID 7854413. S2CID 4335445.
  26. ^ Happe, R.; Roseboom, W.; Pierik, A. & Albracht, S. (1997). "Biological activation of hydrogen". Nature. 385 (6612): 126. doi:10.1038/385126a0. PMID 8990114.
  27. ^ Schneider, K.; Cammack, R.; Schlegel, G. & Hall, D. (1979). "The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus". Biochimica et Biophysica Acta (BBA) - Protein Structure. 578 (2): 445–461. doi:10.1016/0005-2795(79)90175-2. PMID 226163.
  28. ^ Jugder, Bat-Erdene; Chen, Zhiliang; Ping, Darren Tan Tek; Lebhar, Helene; Welch, Jeffrey; Marquis, Christopher P. (2015-03-25). "An analysis of the changes in soluble hydrogenase and global gene expression in Cupriavidus necator (Ralstonia eutropha) H16 grown in heterotrophic diauxic batch culture". Microbial Cell Factories. 14 (1): 42. doi:10.1186/s12934-015-0226-4. ISSN 1475-2859. PMC 4377017. PMID 25880663.
  29. ^ Jugder, Bat-Erdene; Lebhar, Helene; Aguey-Zinsou, Kondo-Francois; Marquis, Christopher P. (2016). "Production and purification of a soluble hydrogenase from Ralstonia eutropha H16 for potential hydrogen fuel cell applications". MethodsX. 3: 242–250. doi:10.1016/j.mex.2016.03.005. ISSN 2215-0161. PMC 4816682. PMID 27077052.
  30. ^ Repaske, R.; Mayer, R. (1976). "Dense Autotrophic Cultures of Alcaligenes eutrophus". Applied and Environmental Microbiology. 32 (4): 592–597. doi:10.1128/AEM.32.4.592-597.1976. PMC 170312. PMID 10840.
  31. ^ Ammann, E.; Reed, L. (1967). "Metabolism of nitrogen compounds by hydrogenomonas eutropha". Biochim. Biophys. Acta. 141 (1): 135–143. doi:10.1016/0304-4165(67)90252-8. PMID 4963807.
  32. ^ Foster, J.; Litchfield, J. (1964). "A Continuous Culture Apparatus for the Microbial Utilization of Hydrogen Produced by Electrolysis of Water in Closed-Cycle Space Systems". Biotechnology and Bioengineering. 6 (4): 441–456. doi:10.1002/bit.260060406. S2CID 84358305.
  33. ^ Ihara, M.; Mishihara, H.; Yoon, K.; Lenz, O.; Friedrich, B.; Nakamoto, H.; Kojima, K.; Honoma, D.; Kamachi, T. & Okura, I. (2006). "Light-driven Hydrogen Production by a Hybrid Complex of a [NiFe]-Hydrogenase and the Cyanobacterial Photosystem I". Photochemistry and Photobiology. 82 (3): 676–682. doi:10.1562/2006-01-16-RA-778. PMID 16542111. S2CID 37919998.
  34. ^ Lutz, B.; Fan, H.; Burgdorf, T. & Friedrich, B. (2005). "Hydrogen Sensing by Enzyme-Catalyzed Electrochemical Detection". Anal. Chem. 77 (15): 4969–4975. doi:10.1021/ac050313i. PMID 16053311.
  35. ^ "Teaching a microbe to make fuel - MIT News Office". Web.mit.edu. Retrieved 2012-08-22.
  36. ^ Li, H.; Opgenorth, P. H.; Wernick, D. G.; Rogers, S.; Wu, T.-Y.; Higashide, W.; Malati, P.; Huo, Y.-X.; Cho, K. M.; Liao, J. C. (2012). "Integrated Electromicrobial Conversion of CO2 to Higher Alcohols". Science. 335 (6076): 1596. doi:10.1126/science.1217643. PMID 22461604. S2CID 24328552.
  37. ^ "Using bacteria to convert CO2 in the air into a polyester". phys.org. doi:10.1073/pnas.2221438120.

External links edit

  • Type strain of Cupriavidus necator at BacDive - the Bacterial Diversity Metadatabase

January 01, 1970
cupriavidus, necator, gram, negative, soil, bacterium, class, betaproteobacteria, scientific, classification, domain, bacteria, phylum, pseudomonadota, class, betaproteobacteria, order, burkholderiales, family, burkholderiaceae, genus, cupriavidus, species, ne. Cupriavidus necator is a Gram negative soil bacterium of the class Betaproteobacteria 1 Cupriavidus necator Scientific classification Domain Bacteria Phylum Pseudomonadota Class Betaproteobacteria Order Burkholderiales Family Burkholderiaceae Genus Cupriavidus Species C necator Binomial name Cupriavidus necator Davis 1969 Yabuuchi et al 1996 Synonyms Ralstonia eutropha Contents 1 Taxonomy 2 Metabolism 3 Hydrogenases 3 1 Regulatory hydrogenase 3 2 Membrane bound hydrogenase 3 3 NAD reducing hydrogenase 3 3 1 Typical anaerobic Ni Fe hydrogenases 3 3 2 C necator oxygen tolerant SH 3 4 Applications 4 Industrial uses 5 References 6 External linksTaxonomy editCupriavidus necator has gone through a series of name changes In the first half of the 20th century many micro organisms were isolated for their ability to use hydrogen Hydrogen metabolizing chemolithotrophic organisms were clustered into the group Hydrogenomonas 2 C necator was originally named Hydrogenomonas eutrophus because it fell under the Hydrogenomonas classification and was well nourished and robust 3 Some of the original H eutrophus cultures isolated were by Bovell and Wilde 4 5 After characterizing cell morphology metabolism and GC content the Hydrogenomonas nomenclature was disbanded because it comprised many species of microorganisms 2 H eutrophus was then renamed Alcaligenes eutropha because it was a micro organism with degenerated peritrichous flagellation 3 6 Investigating phenotype lipid composition fatty acid composition and 16S rRNA analysis A eutropha was found to belong to the genus Ralstonia and named Ralstonia eutropha 1 Upon further study of the genus Ralstonia was found to comprise two phenotypically distinct clusters The new genus Wautersia was created from one of these clusters which included R eutropha In turn R eutropha was renamed Wautersia eutropha 7 Looking at DNA DNA hybridization and phenotype comparison with Cupriavidus necator W eutropha was found to be the same species as previously described C necator Because C necator was named in 1987 far before the name change to R eutropha and W eutropha the name C necator was assigned to R eutropha according to Rule 23a of the International Code of Nomenclature of Bacteria 8 Metabolism editCupriavidus necator is a hydrogen oxidizing bacterium knallgas bacterium capable of growing at the interface of anaerobic and aerobic environments It can easily adapt between heterotrophic and autotrophic lifestyles Both organic compounds and hydrogen can be used as a source of energy 9 C necator can perform aerobic or anaerobic respiration by denitrification of nitrate and or nitrite to nitrogen gas 10 When growing under autotrophic conditions C necator fixes carbon through the reductive pentose phosphate pathway 11 It is known to produce and sequester polyhydroxyalkanoate PHA plastics when exposed to excess amounts of sugar substrate PHA can accumulate to levels around 90 of the cell s dry weight 12 To better characterize the lifestyle of C necator the genomes of two strains have been sequenced 9 13 Hydrogenases editCupriavidus necator can use hydrogen gas as a source of energy when growing under autotrophic conditions It contains four different hydrogenases that have Ni Fe active sites and all perform this reaction 14 15 H2 displaystyle rightleftharpoons nbsp 2H 2e The hydrogenases of C necator are like other typical Ni Fe hydrogenases because they are made up of a large and a small subunit The large subunit is where the Ni Fe active site resides and the small subunit is composed of Fe S clusters 16 However the hydrogenases of C necator are different from typical Ni Fe hydrogenases because they are tolerant to oxygen and are not inhibited by CO 14 While the four hydrogenases perform the same reaction in the cell each hydrogenase is linked to a different cellular process The differences between the regulatory hydrogenase membrane bound hydrogenase soluble hydrogenase and actinobacterial hydrogenase in C necator are described below Regulatory hydrogenase edit The first hydrogenase is a regulatory hydrogenase RH that signals to the cell hydrogen is present The RH is a protein containing large and small Ni Fe hydrogenase subunits attached to a histidine protein kinase subunit 17 The hydrogen gas is oxidized at the Ni Fe center in the large subunit and in turn reduces the Fe S clusters in the small subunit It is unknown whether the electrons are transferred from the Fe S clusters to the protein kinase domain 14 The histidine protein kinase activates a response regulator The response regulator is active in the dephosphorylated form The dephosphorylated response regulator promotes the transcription of the membrane bound hydrogenase and soluble hydrogenase 18 Membrane bound hydrogenase edit The membrane bound hydrogenase MBH is linked to the respiratory chain through a specific cytochrome b related protein in C necator 19 Hydrogen gas is oxidized at the Ni Fe active site in the large subunit and the electrons are shuttled through the Fe S clusters in the small subunit to the cytochrome b like protein 14 The MBH is located on the outer cytoplasmic membrane It recovers energy for the cell by funneling electrons into the respiratory chain and by increasing the proton gradient 19 The MBH in C necator is not inhibited by CO and is tolerant to oxygen 20 NAD reducing hydrogenase edit The NAD reducing hydrogenase soluble hydrogenase SH creates a NADH reducing equivalence by oxidizing hydrogen gas The SH is a heterohexameric protein 21 with two subunits making up the large and small subunits of the Ni Fe hydrogenase and the other two subunits comprising a reductase module similar to the one of Complex I 22 The Ni Fe active site oxidized hydrogen gas which transfers electrons to a FMN a cofactor then to a Fe S cluster relay of the small hydrogenase subunit and the reductase module then to another FMN b cofactor and finally to NAD 14 The reducing equivalences are then used for fixing carbon dioxide when C necator is growing autotrophically The active site of the SH of C necator H16 has been extensively studied because C necator H16 can be produced in large amounts can be genetically manipulated and can be analyzed with spectrographic techniques However no crystal structure is currently available for the C necator H16 soluble hydrogenase in the presence of oxygen to determine the interactions of the active site with the rest of the protein 14 Typical anaerobic Ni Fe hydrogenases edit The Ni Fe hydrogenase from Desulfovibrio vulgaris and D gigas have similar protein structures to each other and represent typical Ni Fe hydrogenases 14 23 24 25 The large subunit contains the Ni Fe active site buried deep in the core of the protein and the small subunit contains Fe S clusters The Ni atom is coordinated to the Desulfovibrio hydrogenase by 4 cysteine ligands Two of these same cysteine ligands also bridge the Fe of the Ni Fe active site 23 24 The Fe atom also contains three ligands one CO and two CN that complete the active site 26 These additional ligands might contribute to the reactivity or help stabilize the Fe atom in the low spin 2 oxidation state 23 Typical NiFe hydrogenases like those of D vulgaris and D gigas are poisoned by oxygen because an oxygen atom binds strongly to the NiFe active site 20 C necator oxygen tolerant SH edit The SH in C necator are unique for other organisms because it is oxygen tolerant 27 The active site of the SH has been studied to learn why this protein is tolerant to oxygen A recent study showed that oxygen tolerance as implemented in the SH is based on a continuous catalytically driven detoxification of O2 Ref missing The genes encoding this SH can be up regulated under heterotrophic growth condition using glycerol in the growth media 28 and this enables aerobic production and purification of the same enzyme 29 Applications edit The oxygen tolerant hydrogenases of C necator have been studied for diverse purposes C necator was studied as an attractive organism to help support life in space It can fix carbon dioxide as a carbon source use the urea in urine as a nitrogen source and use hydrogen as an energy source to create dense cultures that could be used as a source of protein 30 31 Electrolysis of water is one way of creating oxygenic atmosphere in space and C necator was investigated to recycle the hydrogen produced during this process 32 Oxygen tolerant hydrogenases are being used to investigate biofuels Hydrogenases from C necator have been used to coat electrode surfaces to create hydrogen fuel cells tolerant to oxygen and carbon monoxide 20 and to design hydrogen producing light complexes 33 In addition the hydrogenases from C necator have been used to create hydrogen sensors 34 Genetically modified C necator can produce isobutanol from CO2 that can directly substitute or blend with gasoline The organism emits the isobutanol without having to be destroyed to obtain it 35 Industrial uses editResearchers at UCLA have genetically modified a strain of the species C necator formerly known as R eutropha H16 to produce isobutanol from CO2 feedstock using electricity produced by a solar cell The project funded by the U S Dept of Energy is a potential high energy density electrofuel that could use existing infrastructure to replace oil as a transportation fuel 36 Chemical and biomolecular engineers at Korea Advanced Institute of Science and Technology has presented a scalable way to convert CO2 in the air into a polyester by means of the C necator 37 References edit a b Yabuuchi et al 1995 Transfer of two Burkholderia and an Alcaligenes species to Ralstonia gen nov proposal of Ralstonia pickettii Ralston Palleroni and Doudoroff 1973 comb nov Ralstonia solanacearum Smith 1896 comb nov and Ralstonia eutropha Davis 1969 comb nov Microbiol Immunol 39 11 897 904 doi 10 1111 j 1348 0421 1995 tb03275 x PMID 8657018 a b Davis D Doudoroff M amp Stanier R 1969 Proposal to reject the genus Hydrogenomonas Taxonomic implications Int J Syst Bacteriol 19 4 375 390 doi 10 1099 00207713 19 4 375 a b Bowien B Schlegel H 1981 Physiology and biochemistry of aerobic hydrogen oxidizing bacteria Annu Rev Microbiol 35 405 452 doi 10 1146 annurev mi 35 100181 002201 PMID 6271040 Repaske R 1981 Nutritional Requirements forHydrogenomonas eutropha J Bacteriol 83 2 418 422 doi 10 1128 JB 83 2 418 422 1962 PMC 277745 PMID 14491520 Wilde E 1962 Untersuchungen uber Wachstum und Speicherstoffsynthese von Hydrogenomonas eutropha Archiv fur Mikrobiologie 43 2 109 137 doi 10 1007 bf00406429 S2CID 25824711 Davis D Stanier R amp Doudoroff M 1970 Taxonomic Studies on Some Gram Negative Polarly Flagellated Hydrogen Bacteria and Related Species Arch Mikrobiol 70 1 1 13 doi 10 1007 BF00691056 PMID 4987616 S2CID 24798412 Vaneechoutte M Kampfer P De Baere T Falsen E amp Verschraegen G 2004 Wautersia gen nov a novel genus accommodating the phylogenetic lineage including Ralstonia eutropha and related species and proposal of Ralstonia Pseudomonas syzygii Roberts et al 1990 comb nov International Journal of Systematic and Evolutionary Microbiology 54 Pt 2 317 327 doi 10 1099 ijs 0 02754 0 PMID 15023939 Vandamme P Coenye T 2004 Taxonomy of the genus Cupriavidus a tale of lost and found International Journal of Systematic and Evolutionary Microbiology 54 6 2285 2289 doi 10 1099 ijs 0 63247 0 PMID 15545472 a b Pohlmann A Fricke W Reinecke F Kusian B Liesegang H Cramm R Eitinger T Ewering C Potter M Schwartz E Strittmatter A Vob I Gottschalk G Steinbuchel A Friedrich B amp Bowien B 2006 Genome sequence of the bioplastic producing Knallgas bacterium Ralstonia eutropha H16 Nature Biotechnology 24 10 1257 1262 doi 10 1038 nbt1244 hdl 10795 2306 PMID 16964242 Cramm R 2009 Genomic View of Energy Metabolism in Ralstonia eutropha H16 J Mol Microbiol Biotechnol 16 1 2 38 52 doi 10 1159 000142893 PMID 18957861 Bowien B Kusian B 2002 Genetics and control of CO2 assimilation in the chemoautotroph Ralstonia eutropha Arch Microbiol 178 2 85 93 doi 10 1007 s00203 002 0441 3 PMID 12115053 S2CID 26360677 Spiekermann P Rehm B Kalscheuer R Baumeister D amp Steinbuchel A 1999 A sensitive viable colony staining method using Nile red for direct screening of bacteria that accumulate polyhydroxyalkanoic acids and other lipid storage compounds Arch Microbiol 171 2 73 80 doi 10 1007 s002030050681 PMID 9914303 S2CID 206894168 Lykidis A Perez Pantoja D Ledger T Marvomatis K Anderson I Ivanova N Hooper S Lapidus A Lucas A Gonzalez B amp Kyrpides N 2010 Ahmed Niyaz ed The Complete Multipartite Genome Sequence of Cupriavidus necator JMP134 a Versatile Pollutant Degrader PLOS ONE 5 3 1 13 doi 10 1371 journal pone 0009729 PMC 2842291 PMID 20339589 a b c d e f g Burgdorf T Buhrke T van der Linden E Jones A Albracht S amp Friedrich B 2005 NiFe Hydrogenases of Ralstonia eutropha H16 Modular Enzymes for Oxygen Tolerant Biological Hydrogen Oxidation J Mol Microbiol Biotechnol 10 2 4 181 196 doi 10 1159 000091564 PMID 16645314 S2CID 8030367 Schafer Caspar Friedrich Barbel Lenz Oliver 1 September 2013 Novel Oxygen Insensitive Group 5 NiFe Hydrogenase in Ralstonia eutropha Applied and Environmental Microbiology 79 17 5137 5145 doi 10 1128 AEM 01576 13 PMC 3753944 PMID 23793632 Schwartz E Friedrich B 2006 The H2 Metabolizing Prokaryotes Prokaryotes 2 496 563 doi 10 1007 0 387 30742 7 17 ISBN 978 0 387 25492 0 Lenz O Friedrich B 1998 A novel multicomponent regulatory system mediates H2 sensing in Alcaligenes eutrophus PNAS 95 21 12474 12479 doi 10 1073 pnas 95 21 12474 PMC 22855 PMID 9770510 Friedrich B Buhrke T amp Burgdorf T 2005 A hydrogen sensing multiprotein complexcontrols aerobic hydrogen metabolism in Ralstonia eutropha Biochemical Society Transactions 33 Pt 1 97 101 doi 10 1042 BST0330097 PMID 15667276 a b Bernhard M Benelli B Hochkoeppler A Zannoni D amp Friedrich B 1997 Functional and structural role of the cytochrome b subunit of the membrane bound hydrogenase complex of Alcaligenes eutrophus H16 Eur J Biochem 248 1 179 186 doi 10 1111 j 1432 1033 1997 00179 x PMID 9310376 a b c Vincent K Cracknell J Lenz O Zebger I Friedrich B amp Armstrong F 2005 Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels PNAS 102 47 16951 16954 doi 10 1073 pnas 0504499102 PMC 1287975 PMID 16260746 Schneider K Schlegel H 1976 Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16 Biochimica et Biophysica Acta BBA Enzymology 452 1 66 80 doi 10 1016 0005 2744 76 90058 9 PMID 186126 Tran Betcke A Warnecke U Bocker C Zaborosch C amp Friedrich B 1990 Cloning and Nucleotide Sequences of the Genes for the Subunits of NAD Reducing Hydrogenase of Alcaligenes eutrophus H16 Journal of Bacteriology 172 6 2920 2929 doi 10 1128 jb 172 6 2920 2929 1990 PMC 209089 PMID 2188945 a b c Higuchi Yagi T amp Yasuoka N 1997 Unusual ligand structure in Ni Fe active center and an additional Mg site in hydrogenase revealed by high resolution X ray structure analysis Structure 5 12 1671 1680 doi 10 1016 S0969 2126 97 00313 4 PMID 9438867 a b Volbeda A Garcin E Piras C de Lacey A Fernandez V Hatchikian C Frey M amp Fontecilla Camps J 1996 Structure of the NiFe Hydrogenase Active Site Evidence for Biologically Uncommon Fe Ligands J Am Chem Soc 118 51 12989 12996 doi 10 1021 ja962270g Volbeda A Charon M Piras C Hatchikian C Frey M amp Fontecilla Camps J 1995 Crystal structure of the nickel iron hydrogenase from Desulfovibrio gigas Nature 373 6515 580 587 doi 10 1038 373580a0 PMID 7854413 S2CID 4335445 Happe R Roseboom W Pierik A amp Albracht S 1997 Biological activation of hydrogen Nature 385 6612 126 doi 10 1038 385126a0 PMID 8990114 Schneider K Cammack R Schlegel G amp Hall D 1979 The iron sulphur centres of soluble hydrogenase from Alcaligenes eutrophus Biochimica et Biophysica Acta BBA Protein Structure 578 2 445 461 doi 10 1016 0005 2795 79 90175 2 PMID 226163 Jugder Bat Erdene Chen Zhiliang Ping Darren Tan Tek Lebhar Helene Welch Jeffrey Marquis Christopher P 2015 03 25 An analysis of the changes in soluble hydrogenase and global gene expression in Cupriavidus necator Ralstonia eutropha H16 grown in heterotrophic diauxic batch culture Microbial Cell Factories 14 1 42 doi 10 1186 s12934 015 0226 4 ISSN 1475 2859 PMC 4377017 PMID 25880663 Jugder Bat Erdene Lebhar Helene Aguey Zinsou Kondo Francois Marquis Christopher P 2016 Production and purification of a soluble hydrogenase from Ralstonia eutropha H16 for potential hydrogen fuel cell applications MethodsX 3 242 250 doi 10 1016 j mex 2016 03 005 ISSN 2215 0161 PMC 4816682 PMID 27077052 Repaske R Mayer R 1976 Dense Autotrophic Cultures of Alcaligenes eutrophus Applied and Environmental Microbiology 32 4 592 597 doi 10 1128 AEM 32 4 592 597 1976 PMC 170312 PMID 10840 Ammann E Reed L 1967 Metabolism of nitrogen compounds by hydrogenomonas eutropha Biochim Biophys Acta 141 1 135 143 doi 10 1016 0304 4165 67 90252 8 PMID 4963807 Foster J Litchfield J 1964 A Continuous Culture Apparatus for the Microbial Utilization of Hydrogen Produced by Electrolysis of Water in Closed Cycle Space Systems Biotechnology and Bioengineering 6 4 441 456 doi 10 1002 bit 260060406 S2CID 84358305 Ihara M Mishihara H Yoon K Lenz O Friedrich B Nakamoto H Kojima K Honoma D Kamachi T amp Okura I 2006 Light driven Hydrogen Production by a Hybrid Complex of a NiFe Hydrogenase and the Cyanobacterial Photosystem I Photochemistry and Photobiology 82 3 676 682 doi 10 1562 2006 01 16 RA 778 PMID 16542111 S2CID 37919998 Lutz B Fan H Burgdorf T amp Friedrich B 2005 Hydrogen Sensing by Enzyme Catalyzed Electrochemical Detection Anal Chem 77 15 4969 4975 doi 10 1021 ac050313i PMID 16053311 Teaching a microbe to make fuel MIT News Office Web mit edu Retrieved 2012 08 22 Li H Opgenorth P H Wernick D G Rogers S Wu T Y Higashide W Malati P Huo Y X Cho K M Liao J C 2012 Integrated Electromicrobial Conversion of CO2 to Higher Alcohols Science 335 6076 1596 doi 10 1126 science 1217643 PMID 22461604 S2CID 24328552 Using bacteria to convert CO2 in the air into a polyester phys org doi 10 1073 pnas 2221438120 External links editType strain of Cupriavidus necator at BacDive the Bacterial Diversity Metadatabase Retrieved from https en wikipedia org w index php title Cupriavidus necator amp oldid 1206445431, wikipedia, wiki, book, books, library,

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