المؤلفون: Choi, So Young, Rhie, Mi Na, Kim, Hee Taek, Joo, Jeong Chan, Cho, In Jin, Son, Jina, Jo, Seo Young, Sohn, Yu Jung, Baritugo, Kei-Anne, Pyo, Jiwon, Lee, Youngjoon, Lee, Sang Yup, Park, Si Jae

مصطلحات موضوعية: Poly-Beta-Hydroxybutyrate, Recombinant Escherichia-Coli, Fed-Batch Culture, Chain-Length Poly(3-Hydroxyalkanoates), Alcaligenes-Eutrophus H16, Granule-Associated Proteins, Propionate Coa-Transferase, Cell-Density Cultivation, Coenzyme-A Transferase, High-Yield Production

الوصف: As concerns increase regarding sustainable industries and environmental pollutions caused by the accumulation of non-degradable plastic wastes, bio-based polymers, particularly biodegradable plastics, have attracted considerable attention as potential candidates for solving these problems by substituting petroleum-based plastics. Among these candidates, polyhydroxyalkanoates (PHAs), natural polyesters that are synthesized and accumulated in a range of microorganisms, are considered as promising biopolymers since they have biocompatibility, biodegradability, and material properties similar to those of commodity plastics. Accordingly, substantial efforts have been made to gain a better understanding of mechanisms related to the biosynthesis and properties of PHAs and to develop natural and recombinant microorganisms that can efficiently produce PHAs comprising desired monomers with high titer and productivity for industrial applications.Recent advances in biotechnology, including those related to evolutionary engineering, synthetic biology, and systems biology, can provide efficient and effective tools and strategies that reduce time, labor, and costs to develop microbial platform strains that produce desired chemicals and materials. Adopting these technologies in a systematic manner has enabled microbial fermentative production of non-natural polyesters such as poly (lactate) [PLA], poly(lactate-co-glycolate) [PLGA], and even polyesters consisting of aromatic monomers from renewable biomass-derived carbohydrates, which can be widely used in current chemical industries.In this review, we present an overview of strain development for the production of various important natural PHAs, which will give the reader an insight into the recent advances and provide indicators for the future direction of engineering microorganisms as plastic cell factories. On the basis of our current understanding of PHA biosynthesis systems, we discuss recent advances in the approaches adopted for strain development in the production of ...

العلاقة: orcid:0000-0003-0599-3091; NRF-2012M1A2A2026557; NRF-2015M1A2A2035810; NRF-2018M3A9H3020459

الإتاحة: https://doi.org/10.1016/j.ymben.2019.05.009Test
https://espace.library.uq.edu.au/view/UQ:cf4c905Test

المؤلفون: Huisman, Gjalt W., Wonink, Eric, Meima, Rob, Kazemier, Bert, Terpstra, Peter, Witholt, Bernard

المصدر: Huisman , G W , Wonink , E , Meima , R , Kazemier , B , Terpstra , P & Witholt , B 1991 , ' Metabolism of Poly(3-hydroxyalkanoates) (PHAs) by Pseudomonas oleovorans. Identification and Sequences of Genes and Function of the Encoded Proteins in the Synthesis and Degradation of PHA ' , The Journal of Biological Chemistry , vol. 266 , no. 4 , pp. 2191-2198 .

مصطلحات موضوعية: POLY-BETA-HYDROXYBUTYRATE, ALCALIGENES-EUTROPHUS H16, BROAD HOST RANGE, ACETOACETYL-COA REDUCTASE, ESCHERICHIA-COLI, NUCLEOTIDE-SEQUENCE, ALKALINE EXTRACTION, ZOOGLOEA-RAMIGERA, COSMID CLONING, DNA

الوصف: Pseudomonas oleovorans accumulates poly(3-hydroxyalkanoates) (PHAs) after growth on medium chain length hydrocarbons. Large amounts of this polyester are synthesized when cells are grown under nitrogen-limiting conditions. When nitrogen is resupplied in the medium, the accumulated PHA is degraded. In this paper, we describe mutants which are defective in the synthesis or in the degradation of PHA. These mutants were used to select DNA fragments which encode PHA polymerases and a PHA depolymerase. A 25-kilobase (kb) DNA fragment was isolated from P. oleovorans that complements a Pseudomonas putida mutant unable to accumulate PHA. Subcloning resulted in the assignment of a 6.4-kb EcoRI fragment as the pha locus, containing genetic information of PHA synthesis. Mutants in the PHA degradation pathway were also complemented by this fragment, indicating that genes encoding PHA biosynthetic and degradative enzymes are clustered. Analysis of the DNA sequence of the 6.4-kb fragment revealed the presence of two open reading frames encoding PHA polymerases based on homology to the poly(3-hydroxybutyrate) polymerase from Alcaligenes eutrophus. A third open reading frame complemented the PHA degradation mutation and is likely to encode a PHA depolymerase. The presence of two PHA polymerases is due to a 2098-base pair DNA duplication. The PHA polymerases are 53% identical and show 35-40% identity to the poly(3-hydroxybutyrate) polymerase. No clear difference in specificity was found for the PHA polymerases. However, with the pha locus cloned on a multicopy vector, a polymer was accumulated that contains a significantly higher amount of substrate-derived monomers. An increase in the rate of polyester synthesis versus oxidation of the monomers in the beta-oxidation explains these findings.

وصف الملف: application/pdf

العلاقة: https://research.rug.nl/en/publications/988ef9ed-fc7b-49cf-a862-5afb273a5e0bTest

الإتاحة: https://hdl.handle.net/11370/988ef9ed-fc7b-49cf-a862-5afb273a5e0bTest
https://research.rug.nl/en/publications/988ef9ed-fc7b-49cf-a862-5afb273a5e0bTest
https://pure.rug.nl/ws/files/37044617/1991JBiolChemHuisman.pdfTest

المؤلفون: Zhang, Yan, Ashok, Somasundar, Seol, Eunhee, Ainala, Satish Kumar, Lee, Sun-Gu, Madan, Bharat, Xu, Jian-He, Park, Sunghoon

مصطلحات موضوعية: adipic acid, 2-Oxoadipate, 2-Oxoadipate reductase, 2-Oxoglutarate, Alcaligenes eutrophus H16, lactate dehydrogenase

الوصف: Adipic acid is an important monomer for the production of nylon-6,6 polyamide. One novel biological route for the synthesis of adipic acid, which combines the lysine synthetic pathway and glutaconic acid production pathway, has been suggested, but this route has suffered from the lack of an efficient 2-oxoadipate reductase connecting the two pathways or converting 2-oxoadipate to 2-hydroxyadipate. In this study, we report that the lactate dehydrogenase of Alcaligenes eutrophus H16 is a promising catalyst for this reaction. The lactate dehydrogenase gene (Ae-ldhO) was cloned, expressed in Escherichia coli, purified, and characterized. The recombinant enzyme, having a molecular weight of 36.7 kDa, exhibited broad substrate specificity for various 2-oxoacids. NADH was the preferred coenzyme over NADPH for all 2-oxoacids tested. The maximum specific activity of Ae-LdhO on 2-oxoadipate was 454.5 +/- 20.1 U/mg protein at pH 7.0 and 30a"integral. The K (m) values for 2-oxoadipic acid and NADH were 0.32 +/- 0.02 and 0.09 +/- 0.002 mM, respectively. The activity of Ae-LdhO was enhanced in the presence of some metal ions, such as Mg2+, Co2+ or Ni2+, whereas it was completely inhibited by Hg2+, Ag+, Cu2+ and DTT.

العلاقة: BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.19, no.6, pp.1048 - 1057; https://link.springer.com/article/10.1007%2Fs12257-014-0381-1Test; https://scholarworks.unist.ac.kr/handle/201301/25313Test; 3392; 27915; 2-s2.0-84921033736; 000348046500015

الإتاحة: https://doi.org/10.1007/s12257-014-0381-1Test
https://scholarworks.unist.ac.kr/handle/201301/25313Test

المصدر: Biometals. 8(2):149-162

مصطلحات موضوعية: ALCALIGENES-EUTROPHUS H16, NON-IDENTICAL SUBUNITS, HYDROGENASE-DIMER, HYDROGENASE (OR H-2-NAD(+) OXIDOREDUCTASE, EC 1 12 1 2), IRON-SULFUR CENTERS, NOCARDIA OPACA, REDUCING HYDROGENASE, UBIQUINONE REDUCTASE, ELECTRON-PARAMAGNETIC-RES, CATALYTIC PROPERTIES, CLOSTRIDIUM-PASTEURIANUM, EPR AND MOSSBAUER SPECTROSCOPY, AZOTOBACTER-VINELANDII, DIAPHORASE-DIMER, DESULFOVIBRIO-GIGAS

الوصف: The cytoplasmic, tetrameric NAD-linked hydrogenase from Nocardia opaca Ib can be separated in two dimeric substructures, an ay-dimer with NADH:electron acceptor oxidoreductase (diaphorase) activity and a PG-dimer which displays hydrogenase activity with artificial electron carriers, These two dimers were preparatively isolated by a FPLC Mono Q procedure in the absence of nickel and at alkaline pH values, The hydrogenase-active PS-dimer contained, as analyzed by inductively coupled plasma mass spectrometry (TCP-MS), 3.5-3.9 iron atoms and 1.3-1.7 nickel atoms per dimer molecule, EPR and Mossbauer spectra indicated the presence of a [4Fe-4S] cluster, This center turned out to be extremely labile towards oxidants, Oxidation led to irreversible convertion into a [4Fe-4S] form, thus representing an artifact and not a regulatory state of the cluster, The midpoint redox potential of the [4Fe-4S] cluster was determined to be -385 mV, Very weak EPR Ni signals of the PG-dimer were detectable in the oxidized as well as in the reduced state, The diaphorase-active ay-dimer was free of nickel and the iron content corresponded to 11.2-12.8 Fe atoms per dimer molecule, From EPR and Mossbauer measurements it was concluded that this dimer contained two [4Fe-4S] clusters, one [2Fe-2S] and one [3Fe-4S] cluster, In accordance with the results obtained for the diner proteins, for the whole enzyme an iron content of 15.8-16.2 atoms per enzyme molecule have been determined, EPR spectra and spectrum simulations of the native hydrogenase corroborate the cluster assignments of the two dimers: in total the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster and three [4Fe-4S] clusters.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=dris___00893::95e8ae8a061aef0b186248f0aceab9b9Test
https://hdl.handle.net/11370/c9075b61-9fda-4c0e-9a6c-353d6c89187cTest

المؤلفون: Purnell, Matthew P., Petrasovits, Lars A., Nielsen, Lars K., Brumbley, Stevens M.

مصطلحات موضوعية: Biotechnology & Applied Microbiology, Plant Sciences, biofactory, polyhydroxybutyrate, real-time polymerase chain reaction, Saccharum, transgenic sugarcane, Poly-beta-hydroxybutyrate, Alcaligenes-eutrophus H16, Transplastomic Tobacco, Transgenic Tobacco, Expression, Plants, Gene, Ketothiolase, Arabidopsis, Biosynthesis, 270899 Biotechnology not elsewhere classified, C1, 780105 Biological sciences

الوصف: We report here the results from a glasshouse trial of several transgenic sugarcane (Saccharum spp. hybrids) lines accumulating the bacterial polyester polyhydroxybutyrate (PHB) in plastids. The aims of the trial were to characterize the spatio-temporal pattern of PHB accumulation at a whole-plant level, to identify factors limiting PHB production and to determine whether agronomic performance was affected adversely by PHB accumulation. Statistical analysis showed that a vertical PHB concentration gradient existed throughout the plant, the polymer concentration being lowest in the youngest leaves and increasing with leaf age. In addition, there was a horizontal gradient along the length of a leaf, with the PHB concentration increasing from the youngest part of the leaf (the base) to the oldest (the tip). The rank order of the lines did not change over time. Moreover, there was a uniform spatio-temporal pattern of relative PHB accumulation among the lines, despite the fact that they showed marked differences in absolute PHB concentration. Molecular analysis revealed that the expression of the transgenes encoding the PHB biosynthesis enzymes was apparently coordinated, and that there were good correlations between PHB concentration and the abundance of the PHB biosynthesis enzymes. The maximum recorded PHB concentration, 1.77% of leaf dry weight, did not confer an agronomic penalty. The plant height, total aerial biomass and culm-internode sugar content were not affected relative to controls. Although moderate PHB concentrations were achieved in leaves, the maximum total-plant PHB yield was only 0.79% (11.9 g PHB in 1.51 kg dry weight). We combine the insights from our statistical and molecular analyses to discuss possible strategies for increasing the yield of PHB in sugarcane.

العلاقة: orcid:0000-0001-8191-3511

الإتاحة: https://doi.org/10.1111/j.1467-7652.2006.00230.xTest
https://espace.library.uq.edu.au/view/UQ:127650Test

المصدر: The Journal of Biological Chemistry. 266(4):2191-2198

مصطلحات موضوعية: ALCALIGENES-EUTROPHUS H16, ALKALINE EXTRACTION, ESCHERICHIA-COLI, NUCLEOTIDE-SEQUENCE, ACETOACETYL-COA REDUCTASE, COSMID CLONING, BROAD HOST RANGE, POLY-BETA-HYDROXYBUTYRATE, DNA, ZOOGLOEA-RAMIGERA

الوصف: Pseudomonas oleovorans accumulates poly(3-hydroxyalkanoates) (PHAs) after growth on medium chain length hydrocarbons. Large amounts of this polyester are synthesized when cells are grown under nitrogen-limiting conditions. When nitrogen is resupplied in the medium, the accumulated PHA is degraded. In this paper, we describe mutants which are defective in the synthesis or in the degradation of PHA. These mutants were used to select DNA fragments which encode PHA polymerases and a PHA depolymerase. A 25-kilobase (kb) DNA fragment was isolated from P. oleovorans that complements a Pseudomonas putida mutant unable to accumulate PHA. Subcloning resulted in the assignment of a 6.4-kb EcoRI fragment as the pha locus, containing genetic information of PHA synthesis. Mutants in the PHA degradation pathway were also complemented by this fragment, indicating that genes encoding PHA biosynthetic and degradative enzymes are clustered. Analysis of the DNA sequence of the 6.4-kb fragment revealed the presence of two open reading frames encoding PHA polymerases based on homology to the poly(3-hydroxybutyrate) polymerase from Alcaligenes eutrophus. A third open reading frame complemented the PHA degradation mutation and is likely to encode a PHA depolymerase. The presence of two PHA polymerases is due to a 2098-base pair DNA duplication. The PHA polymerases are 53% identical and show 35-40% identity to the poly(3-hydroxybutyrate) polymerase. No clear difference in specificity was found for the PHA polymerases. However, with the pha locus cloned on a multicopy vector, a polymer was accumulated that contains a significantly higher amount of substrate-derived monomers. An increase in the rate of polyester synthesis versus oxidation of the monomers in the beta-oxidation explains these findings.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=dris___01423::9e664b59f9dc59541f247f1d5e157445Test
https://research.rug.nl/en/publications/988ef9ed-fc7b-49cf-a862-5afb273a5e0bTest

المؤلفون: Bert Kazemier, Gjalt W. Huisman, Rob Meima, Eric Wonink, Bernard Witholt, Peter Terpstra

المساهمون: Groningen Biomolecular Sciences and Biotechnology

المصدر: The Journal of Biological Chemistry, 266(4), 2191-2198. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

مصطلحات موضوعية: Nitrogen, Polyesters, ACETOACETYL-COA REDUCTASE, Molecular Sequence Data, Restriction Mapping, Mutant, chemical and pharmacologic phenomena, Pseudomonas oleovorans, Molecular cloning, Biochemistry, Open Reading Frames, chemistry.chemical_compound, Bacterial Proteins, NUCLEOTIDE-SEQUENCE, Pseudomonas, Sequence Homology, Nucleic Acid, Animals, Humans, POLY-BETA-HYDROXYBUTYRATE, Amino Acid Sequence, Cloning, Molecular, Molecular Biology, Polymerase, ALCALIGENES-EUTROPHUS H16, Base Sequence, biology, COSMID CLONING, Nucleic acid sequence, BROAD HOST RANGE, DNA, Cell Biology, biology.organism_classification, Hydrocarbons, Pseudomonas putida, ALKALINE EXTRACTION, chemistry, ESCHERICHIA-COLI, PHA granule, Mutation, biology.protein, Nucleic Acid Conformation, ZOOGLOEA-RAMIGERA, Acyltransferases

الوصف: Pseudomonas oleovorans accumulates poly(3-hydroxyalkanoates) (PHAs) after growth on medium chain length hydrocarbons. Large amounts of this polyester are synthesized when cells are grown under nitrogen-limiting conditions. When nitrogen is resupplied in the medium, the accumulated PHA is degraded. In this paper, we describe mutants which are defective in the synthesis or in the degradation of PHA. These mutants were used to select DNA fragments which encode PHA polymerases and a PHA depolymerase. A 25-kilobase (kb) DNA fragment was isolated from P. oleovorans that complements a Pseudomonas putida mutant unable to accumulate PHA. Subcloning resulted in the assignment of a 6.4-kb EcoRI fragment as the pha locus, containing genetic information for PHA synthesis. Mutants in the PHA degradation pathway were also complemented by this fragment, indicating that genes encoding PHA biosynthetic and degradative enzymes are clustered. Analysis of the DNA sequence of the 6.4-kb fragment revealed the presence of two open reading frames encoding PHA polymerases based on homology to the poly(3-hydroxybutyrate) polymerase from Alcaligenes eutrophus. A third open reading frame complemented the PHA degradation mutation and is likely to encode a PHA depolymerase. The presence of two PHA polymerases is due to a 2098-base pair DNA duplication. The PHA polymerases are 53% identical and show 35-40% identity to the poly(3-hydroxybutyrate) polymerase. No clear difference in specificity was found for the PHA polymerases. However, with the pha locus cloned on a multicopy vector, a polymer was accumulated that contains a significantly higher amount of substrate-derived monomers. An increase in the rate of polyester synthesis versus oxidation of the monomers in the beta-oxidation explains these findings.

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3bb55f3e71cb00713ee37f5a53efa2dTest
https://doi.org/10.1016/s0021-9258Test(18)52227-4

المؤلفون: Van Wegen, RJ, Ling, Y, Middelberg, APJ

مصطلحات موضوعية: polyhydroxyalkanoate, Escherichia coli, economic analysis, dairy whey, fermentation, Poly-Beta-Hydroxybutyrate, Alcaligenes-Eutrophus H16, Poly(3-Hydroxybutyric Acid), Carbon-Sources, Protein, Poly(3-Hydroxybutyrate-Co-3-Hydroxyvalerate), Biosynthesis, Recovery, Granules

الإتاحة: https://doi.org/10.1205/026387698524848Test
https://espace.library.uq.edu.au/view/UQ:294564Test

المؤلفون: Friedrich, B., Schlegel, H.G.

المصدر: Arch. Microbiol. 103, 141-149 (1975)

مصطلحات موضوعية: Accumulation Of Prephenic And Chorismic Acid, Alcaligenes Eutrophus H16, Auxotrophic Mutants, Phenylalanine-tyrosine Biosynthesis

الوصف: 1. Mutants derived from the hydrogen bacterium Alcaligenes eutrophus strain H16 auxotrophic for phenylalanine and tyrosine were isolated employing mutagenic agents (EMS, nitrite), the colistine counterselection technique and the "pin-point" isolation method. Three different types of mutants were found: (1) Mutants, requiring phenylalanine or phenylpyruvate for growth, were affected in chorismate mutase as well as prephenate dehydratase. Both activities were regained by reversion to prototrophy. The auxotrophic strains accumulated chorismic acid. (2) Strains with a growth response similar to that of the first group lacked only prephenate dehydratase activity which was partially regained by reversion. Chorismate mutase and prephenate dehydrogenase were derepressed up to two-fold. Mutants grown in minimal medium excreted prephenic acid. (3) The third type of mutants required phenylalanine or phenylpyruvate and grew slowly when supplemented with chorismate or prephenate. The enzymes involved in the specific pathway of phenylalanine and tyrosine were found to be present. Some of them were even more active than in the wild-type. 2. Mutants accumulating chorismic acid or prephenic acid were able to grow on minimal medium when incubated long enough. The chemical instability of the excretion products resulted in their nonenzymatic conversion to subsequent intermediates which were taken up by the cells, allowing growth. 3. A method is described for preparing barium prephenate using the auxotrophic mutant 6B-1 derived from A. eutrophus H16. Prephenic acid, excreted by this strain, was obtained from the culture filtrate with a purity of at least 70% and a yield of approximately 180 mg per 2 l of medium.

وصف الملف: application/pdf

العلاقة: info:eu-repo/semantics/altIdentifier/wos/undefined; info:eu-repo/semantics/altIdentifier/isbn/0302-8933; info:eu-repo/semantics/altIdentifier/pissn/0003-9276; info:eu-repo/semantics/altIdentifier/e; https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=33026Test; urn:isbn:0302-8933; urn:issn:0003-9276; urn:issn:1432-072X

الإتاحة: https://doi.org/10.1007/BF00436341Test
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=33026Test

المؤلفون: ZABOROSCH, C, KOSTER, M, BILL, E, SCHNEIDER, K, SCHLEGEL, HG, TRAUTWEIN, AX

المصدر: ZABOROSCH , C , KOSTER , M , BILL , E , SCHNEIDER , K , SCHLEGEL , HG & TRAUTWEIN , AX 1995 , ' EPR AND MOSSBAUER SPECTROSCOPIC STUDIES ON THE TETRAMERIC, NAD-LINKED HYDROGENASE OF NOCARDIA-OPACA-1B AND ITS 2 DIMERS .1. THE BETA-DELTA-DIMER - A PROTOTYPE OF A SIMPLE HYDROGENASE ' , Biometals , vol. 8 , no. 2 , pp. 149-162 . ; ISSN:0966-0844

مصطلحات موضوعية: HYDROGENASE (OR H-2-NAD(+) OXIDOREDUCTASE, EC 1 12 1 2), NOCARDIA OPACA, DIAPHORASE-DIMER, HYDROGENASE-DIMER, EPR AND MOSSBAUER SPECTROSCOPY, ALCALIGENES-EUTROPHUS H16, ELECTRON-PARAMAGNETIC-RES, IRON-SULFUR CENTERS, NON-IDENTICAL SUBUNITS, DESULFOVIBRIO-GIGAS, REDUCING HYDROGENASE, CLOSTRIDIUM-PASTEURIANUM, AZOTOBACTER-VINELANDII, UBIQUINONE REDUCTASE, CATALYTIC PROPERTIES

الوصف: The cytoplasmic, tetrameric NAD-linked hydrogenase from Nocardia opaca Ib can be separated in two dimeric substructures, an ay-dimer with NADH:electron acceptor oxidoreductase (diaphorase) activity and a PG-dimer which displays hydrogenase activity with artificial electron carriers, These two dimers were preparatively isolated by a FPLC Mono Q procedure in the absence of nickel and at alkaline pH values, The hydrogenase-active PS-dimer contained, as analyzed by inductively coupled plasma mass spectrometry (TCP-MS), 3.5-3.9 iron atoms and 1.3-1.7 nickel atoms per dimer molecule, EPR and Mossbauer spectra indicated the presence of a [4Fe-4S] cluster, This center turned out to be extremely labile towards oxidants, Oxidation led to irreversible convertion into a [4Fe-4S] form, thus representing an artifact and not a regulatory state of the cluster, The midpoint redox potential of the [4Fe-4S] cluster was determined to be -385 mV, Very weak EPR Ni signals of the PG-dimer were detectable in the oxidized as well as in the reduced state, The diaphorase-active ay-dimer was free of nickel and the iron content corresponded to 11.2-12.8 Fe atoms per dimer molecule, From EPR and Mossbauer measurements it was concluded that this dimer contained two [4Fe-4S] clusters, one [2Fe-2S] and one [3Fe-4S] cluster, In accordance with the results obtained for the diner proteins, for the whole enzyme an iron content of 15.8-16.2 atoms per enzyme molecule have been determined, EPR spectra and spectrum simulations of the native hydrogenase corroborate the cluster assignments of the two dimers: in total the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster and three [4Fe-4S] clusters.

الإتاحة: http://hdl.handle.net/11370/c9075b61-9fda-4c0e-9a6c-353d6c89187cTest
https://research.rug.nl/en/publications/epr-and-mossbauer-spectroscopic-studies-on-the-tetrameric-nadlinked-hydrogenase-of-nocardiaopaca1b-and-its-2-dimers-1-the-betadeltadimer--a-prototype-of-a-simple-hydrogenaseTest(c9075b61-9fda-4c0e-9a6c-353d6c89187c).html