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You searched for subject:(Enzyme reaction kinetics). Showing records 1 – 13 of 13 total matches.

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East Tennessee State University

1. Kalu, Chimdi Eke. Synthesis and Evaluation of 1,2,4-oxadiazolidinones: The Search for A Potential Non-β-lactam β-lactamase Inhibitors.

Degree: MS, Chemistry, 2019, East Tennessee State University

  β-lactam antibiotics have been the most widely used drug of choice to combat infectious disease caused by bacteria. Unfortunately, their effectiveness is drastically threatened… (more)

Subjects/Keywords: Antibiotic resistance; β-Lactamases inhibitors; Nitrones; Cycloaddition Reaction; Oxadiazolidinones and Enzyme kinetics; Organic Chemistry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Kalu, C. E. (2019). Synthesis and Evaluation of 1,2,4-oxadiazolidinones: The Search for A Potential Non-β-lactam β-lactamase Inhibitors. (Masters Thesis). East Tennessee State University. Retrieved from https://dc.etsu.edu/etd/3578

Chicago Manual of Style (16th Edition):

Kalu, Chimdi Eke. “Synthesis and Evaluation of 1,2,4-oxadiazolidinones: The Search for A Potential Non-β-lactam β-lactamase Inhibitors.” 2019. Masters Thesis, East Tennessee State University. Accessed August 23, 2019. https://dc.etsu.edu/etd/3578.

MLA Handbook (7th Edition):

Kalu, Chimdi Eke. “Synthesis and Evaluation of 1,2,4-oxadiazolidinones: The Search for A Potential Non-β-lactam β-lactamase Inhibitors.” 2019. Web. 23 Aug 2019.

Vancouver:

Kalu CE. Synthesis and Evaluation of 1,2,4-oxadiazolidinones: The Search for A Potential Non-β-lactam β-lactamase Inhibitors. [Internet] [Masters thesis]. East Tennessee State University; 2019. [cited 2019 Aug 23]. Available from: https://dc.etsu.edu/etd/3578.

Council of Science Editors:

Kalu CE. Synthesis and Evaluation of 1,2,4-oxadiazolidinones: The Search for A Potential Non-β-lactam β-lactamase Inhibitors. [Masters Thesis]. East Tennessee State University; 2019. Available from: https://dc.etsu.edu/etd/3578


University of Texas – Austin

2. Agarwal, Animesh. Stochastic modeling and simulation of biochemical reaction kinetics.

Degree: Biomedical Engineering, 2011, University of Texas – Austin

 Biochemical reactions make up most of the activity in a cell. There is inherent stochasticity in the kinetic behavior of biochemical reactions which in turn… (more)

Subjects/Keywords: Stochastic simulation; Molecular signaling; Enzyme reaction kinetics; Quasi-steady state approximation; Dimensionality reduction; Bistable molecular switch; Gillespie Algorithm

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APA (6th Edition):

Agarwal, A. (2011). Stochastic modeling and simulation of biochemical reaction kinetics. (Thesis). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2011-08-4067

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Agarwal, Animesh. “Stochastic modeling and simulation of biochemical reaction kinetics.” 2011. Thesis, University of Texas – Austin. Accessed August 23, 2019. http://hdl.handle.net/2152/ETD-UT-2011-08-4067.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Agarwal, Animesh. “Stochastic modeling and simulation of biochemical reaction kinetics.” 2011. Web. 23 Aug 2019.

Vancouver:

Agarwal A. Stochastic modeling and simulation of biochemical reaction kinetics. [Internet] [Thesis]. University of Texas – Austin; 2011. [cited 2019 Aug 23]. Available from: http://hdl.handle.net/2152/ETD-UT-2011-08-4067.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Agarwal A. Stochastic modeling and simulation of biochemical reaction kinetics. [Thesis]. University of Texas – Austin; 2011. Available from: http://hdl.handle.net/2152/ETD-UT-2011-08-4067

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Brno University of Technology

3. Pospíšilová, Michaela. Elektrochemická impedanční analýza enzymové reakce .

Degree: 2015, Brno University of Technology

 Aplikace elektrochemické impedanční spektroskopie (EIS) pro studium redoxních enzymových reakcí byla již popsána. Impedanční měření jsou velmi citlivé na změny na rozhraní mezi elektrodou a… (more)

Subjects/Keywords: biosenzory; impedance; enzymy; kinetika enzymových reakcí; elektrochemická impedanční spektroskopie.; biosensors; impedance analysis; enzymes; kinetics of enzyme reaction; elektrochemical impedance spektroskopy.

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APA (6th Edition):

Pospíšilová, M. (2015). Elektrochemická impedanční analýza enzymové reakce . (Thesis). Brno University of Technology. Retrieved from http://hdl.handle.net/11012/40712

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Pospíšilová, Michaela. “Elektrochemická impedanční analýza enzymové reakce .” 2015. Thesis, Brno University of Technology. Accessed August 23, 2019. http://hdl.handle.net/11012/40712.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Pospíšilová, Michaela. “Elektrochemická impedanční analýza enzymové reakce .” 2015. Web. 23 Aug 2019.

Vancouver:

Pospíšilová M. Elektrochemická impedanční analýza enzymové reakce . [Internet] [Thesis]. Brno University of Technology; 2015. [cited 2019 Aug 23]. Available from: http://hdl.handle.net/11012/40712.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Pospíšilová M. Elektrochemická impedanční analýza enzymové reakce . [Thesis]. Brno University of Technology; 2015. Available from: http://hdl.handle.net/11012/40712

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


The Ohio State University

4. Mehta, Bhavya Chandrakant. Optimization of enzyme dissociation process based on reaction diffusion model to predict time of tissue digestion.

Degree: PhD, Chemical Engineering, 2006, The Ohio State University

  With the advent of highly sensitive molecular analysis technologies, it is possible to study increasingly complex cellular processes in diseases like cancer. However, the… (more)

Subjects/Keywords: Breast Tumor; Collagen; Collagenase; Enzyme Digestion; Enzyme kinetics; Reaction diffusion model

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APA (6th Edition):

Mehta, B. C. (2006). Optimization of enzyme dissociation process based on reaction diffusion model to predict time of tissue digestion. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1142575553

Chicago Manual of Style (16th Edition):

Mehta, Bhavya Chandrakant. “Optimization of enzyme dissociation process based on reaction diffusion model to predict time of tissue digestion.” 2006. Doctoral Dissertation, The Ohio State University. Accessed August 23, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=osu1142575553.

MLA Handbook (7th Edition):

Mehta, Bhavya Chandrakant. “Optimization of enzyme dissociation process based on reaction diffusion model to predict time of tissue digestion.” 2006. Web. 23 Aug 2019.

Vancouver:

Mehta BC. Optimization of enzyme dissociation process based on reaction diffusion model to predict time of tissue digestion. [Internet] [Doctoral dissertation]. The Ohio State University; 2006. [cited 2019 Aug 23]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1142575553.

Council of Science Editors:

Mehta BC. Optimization of enzyme dissociation process based on reaction diffusion model to predict time of tissue digestion. [Doctoral Dissertation]. The Ohio State University; 2006. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1142575553

5. Kaplan, Elise. Aminoglycoside modifying enzymes involved in antibiotic resistance : functional and structural studies : Enzymes de modification des aminoglycosides impliquées dans la résistance aux antibiotiques : études fonctionnelles et structurales.

Degree: Docteur es, Biologie Santé, 2015, Montpellier

L'émergence de bactéries résistantes aux antibiotiques constitue un problème majeur de santé publique responsable d'un nombre croissant de décès, surtout dans les hôpitaux. La résistance… (more)

Subjects/Keywords: Résistance aux antibiotiques; Aminoglycoside phosphotransférases; Cristallographie aux rayons X; Cinétique enzymatique; Inhibiteurs allostériques; Mécanisme réactionnel; Antibiotic resistance; Aminoglycoside phosphotransferases; X-Ray crystallography; Enzyme kinetics; Allosteric inhibitors; Reaction mechanism

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APA (6th Edition):

Kaplan, E. (2015). Aminoglycoside modifying enzymes involved in antibiotic resistance : functional and structural studies : Enzymes de modification des aminoglycosides impliquées dans la résistance aux antibiotiques : études fonctionnelles et structurales. (Doctoral Dissertation). Montpellier. Retrieved from http://www.theses.fr/2015MONTT006

Chicago Manual of Style (16th Edition):

Kaplan, Elise. “Aminoglycoside modifying enzymes involved in antibiotic resistance : functional and structural studies : Enzymes de modification des aminoglycosides impliquées dans la résistance aux antibiotiques : études fonctionnelles et structurales.” 2015. Doctoral Dissertation, Montpellier. Accessed August 23, 2019. http://www.theses.fr/2015MONTT006.

MLA Handbook (7th Edition):

Kaplan, Elise. “Aminoglycoside modifying enzymes involved in antibiotic resistance : functional and structural studies : Enzymes de modification des aminoglycosides impliquées dans la résistance aux antibiotiques : études fonctionnelles et structurales.” 2015. Web. 23 Aug 2019.

Vancouver:

Kaplan E. Aminoglycoside modifying enzymes involved in antibiotic resistance : functional and structural studies : Enzymes de modification des aminoglycosides impliquées dans la résistance aux antibiotiques : études fonctionnelles et structurales. [Internet] [Doctoral dissertation]. Montpellier; 2015. [cited 2019 Aug 23]. Available from: http://www.theses.fr/2015MONTT006.

Council of Science Editors:

Kaplan E. Aminoglycoside modifying enzymes involved in antibiotic resistance : functional and structural studies : Enzymes de modification des aminoglycosides impliquées dans la résistance aux antibiotiques : études fonctionnelles et structurales. [Doctoral Dissertation]. Montpellier; 2015. Available from: http://www.theses.fr/2015MONTT006


University of Arizona

6. Bhattacharyya, Anjan Kumar. Intramolecular and intracomplex electron transfer in water soluble redox proteins.

Degree: 1988, University of Arizona

 Electron transfer to and between the redox centers of milk xanthine oxidase was investigated by laser flash-photolysis. Evidence is presented for slow equilibration of electrons… (more)

Subjects/Keywords: Charge transfer.; Oxidation-reduction reaction.; Electron donor-acceptor complexes.; Enzyme kinetics.

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APA (6th Edition):

Bhattacharyya, A. K. (1988). Intramolecular and intracomplex electron transfer in water soluble redox proteins. (Doctoral Dissertation). University of Arizona. Retrieved from http://hdl.handle.net/10150/184339

Chicago Manual of Style (16th Edition):

Bhattacharyya, Anjan Kumar. “Intramolecular and intracomplex electron transfer in water soluble redox proteins. ” 1988. Doctoral Dissertation, University of Arizona. Accessed August 23, 2019. http://hdl.handle.net/10150/184339.

MLA Handbook (7th Edition):

Bhattacharyya, Anjan Kumar. “Intramolecular and intracomplex electron transfer in water soluble redox proteins. ” 1988. Web. 23 Aug 2019.

Vancouver:

Bhattacharyya AK. Intramolecular and intracomplex electron transfer in water soluble redox proteins. [Internet] [Doctoral dissertation]. University of Arizona; 1988. [cited 2019 Aug 23]. Available from: http://hdl.handle.net/10150/184339.

Council of Science Editors:

Bhattacharyya AK. Intramolecular and intracomplex electron transfer in water soluble redox proteins. [Doctoral Dissertation]. University of Arizona; 1988. Available from: http://hdl.handle.net/10150/184339


University of Florida

7. Carrigan, Matthew A. Searching molecular landscapes for the evolution of primal catalysts : in vitro selection of DNA-based ribonucleases.

Degree: PhD, Medical Sciences – Neuroscience, 2002, University of Florida

Subjects/Keywords: Catalysts; Enzyme substrates; Enzymes; Kinetics; Lasers; Libraries; Molecules; Nucleotides; Polymerase chain reaction; Population distributions

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APA (6th Edition):

Carrigan, M. A. (2002). Searching molecular landscapes for the evolution of primal catalysts : in vitro selection of DNA-based ribonucleases. (Doctoral Dissertation). University of Florida. Retrieved from http://ufdc.ufl.edu/AA00022313

Chicago Manual of Style (16th Edition):

Carrigan, Matthew A. “Searching molecular landscapes for the evolution of primal catalysts : in vitro selection of DNA-based ribonucleases.” 2002. Doctoral Dissertation, University of Florida. Accessed August 23, 2019. http://ufdc.ufl.edu/AA00022313.

MLA Handbook (7th Edition):

Carrigan, Matthew A. “Searching molecular landscapes for the evolution of primal catalysts : in vitro selection of DNA-based ribonucleases.” 2002. Web. 23 Aug 2019.

Vancouver:

Carrigan MA. Searching molecular landscapes for the evolution of primal catalysts : in vitro selection of DNA-based ribonucleases. [Internet] [Doctoral dissertation]. University of Florida; 2002. [cited 2019 Aug 23]. Available from: http://ufdc.ufl.edu/AA00022313.

Council of Science Editors:

Carrigan MA. Searching molecular landscapes for the evolution of primal catalysts : in vitro selection of DNA-based ribonucleases. [Doctoral Dissertation]. University of Florida; 2002. Available from: http://ufdc.ufl.edu/AA00022313


Swedish University of Agricultural Sciences

8. Pavlova, Alona. Mechanism of action of mammalian cystatins.

Degree: 2003, Swedish University of Agricultural Sciences

 Mammalian cystatins are tight-binding, reversible inhibitors of potentially destructive cysteine proteases, both endogenous and exogenous. The N-terminal region residues, Ile2 and especially Pro3, and the… (more)

Subjects/Keywords: molecular biology; inhibition; enzyme inhibitors; cysteine protease; papain; cathepsin; inhibition; cystatin; affinity; binding kinetics; two-step reaction mechanism; occluding loop; binding loop

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APA (6th Edition):

Pavlova, A. (2003). Mechanism of action of mammalian cystatins. (Doctoral Dissertation). Swedish University of Agricultural Sciences. Retrieved from http://pub.epsilon.slu.se/300/

Chicago Manual of Style (16th Edition):

Pavlova, Alona. “Mechanism of action of mammalian cystatins.” 2003. Doctoral Dissertation, Swedish University of Agricultural Sciences. Accessed August 23, 2019. http://pub.epsilon.slu.se/300/.

MLA Handbook (7th Edition):

Pavlova, Alona. “Mechanism of action of mammalian cystatins.” 2003. Web. 23 Aug 2019.

Vancouver:

Pavlova A. Mechanism of action of mammalian cystatins. [Internet] [Doctoral dissertation]. Swedish University of Agricultural Sciences; 2003. [cited 2019 Aug 23]. Available from: http://pub.epsilon.slu.se/300/.

Council of Science Editors:

Pavlova A. Mechanism of action of mammalian cystatins. [Doctoral Dissertation]. Swedish University of Agricultural Sciences; 2003. Available from: http://pub.epsilon.slu.se/300/

9. Kim, Hak Joong, 1974-. Investigation of the post-polyketide synthase (PKS) modifications during spinosyn A biosynthesis in Saccharopolyspora spinosa.

Degree: Chemistry, 2010, University of Texas – Austin

 Diverse biological activities of polyketide natural products are often associated with specific structural motifs, biosynthetically introduced after construction of the polyketide core. Therefore, investigation of… (more)

Subjects/Keywords: Polyketide; Biosynthesis; Spinosyn; Methyltransferase; Diels-Alderase; Rauhut-Currier reaction; Intramolecular C-C bond formation; Kinetics; Enzyme mechanism

enzyme catalysis. viii Table of Contents List of Tables… …Novel Enzyme Chemistry… …9 1.4.1. Group Transfer Reaction… …166 4.3.3. Mechanistic Consideration and Quatitative Assessment of the SpnM reaction… …Cycloaddition Step and Mechanistic Consideration of the SpnF Reaction… 

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APA (6th Edition):

Kim, Hak Joong, 1. (2010). Investigation of the post-polyketide synthase (PKS) modifications during spinosyn A biosynthesis in Saccharopolyspora spinosa. (Thesis). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/22143

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Kim, Hak Joong, 1974-. “Investigation of the post-polyketide synthase (PKS) modifications during spinosyn A biosynthesis in Saccharopolyspora spinosa.” 2010. Thesis, University of Texas – Austin. Accessed August 23, 2019. http://hdl.handle.net/2152/22143.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Kim, Hak Joong, 1974-. “Investigation of the post-polyketide synthase (PKS) modifications during spinosyn A biosynthesis in Saccharopolyspora spinosa.” 2010. Web. 23 Aug 2019.

Vancouver:

Kim, Hak Joong 1. Investigation of the post-polyketide synthase (PKS) modifications during spinosyn A biosynthesis in Saccharopolyspora spinosa. [Internet] [Thesis]. University of Texas – Austin; 2010. [cited 2019 Aug 23]. Available from: http://hdl.handle.net/2152/22143.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Kim, Hak Joong 1. Investigation of the post-polyketide synthase (PKS) modifications during spinosyn A biosynthesis in Saccharopolyspora spinosa. [Thesis]. University of Texas – Austin; 2010. Available from: http://hdl.handle.net/2152/22143

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


ETH Zürich

10. Scheller, Silvan. Methyl-coenzyme M reductase: Mechanistic studies with ²H and ¹³C labels.

Degree: 2011, ETH Zürich

Subjects/Keywords: DEUTERIUM (HYDROGEN ISOTOPE); KOHLENSTOFFISOTOPE; REACTION MECHANISMS + REACTIVITY (CHEMICAL KINETICS); ENZYMAKTIVITÄT (BIOCHEMIE); METHYLREDUKTASE (ENZYME); METHYL REDUCTASE (ENZYMES); REAKTIONSMECHANISMEN + REAKTIVITÄT (CHEMISCHE KINETIK); CARBON/ISOTOPES; DEUTERIUM (WASSERSTOFFISOTOP); ENZYMATIC ACTIVITY (BIOCHEMISTRY); METHANBILDUNG, METHANPRODUZIERENDE MIKROORGANISMEN (MIKROBIOLOGIE); METHANOGENESIS, METHANE PRODUCING MICROORGANISMS (MICROBIOLOGY); info:eu-repo/classification/ddc/570; Life sciences

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APA (6th Edition):

Scheller, S. (2011). Methyl-coenzyme M reductase: Mechanistic studies with ²H and ¹³C labels. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/41504

Chicago Manual of Style (16th Edition):

Scheller, Silvan. “Methyl-coenzyme M reductase: Mechanistic studies with ²H and ¹³C labels.” 2011. Doctoral Dissertation, ETH Zürich. Accessed August 23, 2019. http://hdl.handle.net/20.500.11850/41504.

MLA Handbook (7th Edition):

Scheller, Silvan. “Methyl-coenzyme M reductase: Mechanistic studies with ²H and ¹³C labels.” 2011. Web. 23 Aug 2019.

Vancouver:

Scheller S. Methyl-coenzyme M reductase: Mechanistic studies with ²H and ¹³C labels. [Internet] [Doctoral dissertation]. ETH Zürich; 2011. [cited 2019 Aug 23]. Available from: http://hdl.handle.net/20.500.11850/41504.

Council of Science Editors:

Scheller S. Methyl-coenzyme M reductase: Mechanistic studies with ²H and ¹³C labels. [Doctoral Dissertation]. ETH Zürich; 2011. Available from: http://hdl.handle.net/20.500.11850/41504


University of Florida

11. Rao, Chetana Manohar, 1963-. A Detailed investigation into the enzymatic specificity of porcine pepsin.

Degree: 1994, University of Florida

Subjects/Keywords: Active sites; Amino acids; Biochemistry; Electrostatics; Enzyme substrates; Enzymes; Gels; Kinetics; pH; Polymerase chain reaction; Binding Sites ( mesh ); Department of Biochemistry and Molecular Biology thesis Ph.D ( mesh ); Mutagenesis, Site-Directed ( mesh ); Pepsin A  – metabolism ( mesh ); Pepsin A  – pharmacokinetics ( mesh ); Structure-Activity Relationship ( mesh ); Substrate Specificity ( mesh )

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APA (6th Edition):

Rao, Chetana Manohar, 1. (1994). A Detailed investigation into the enzymatic specificity of porcine pepsin. (Thesis). University of Florida. Retrieved from http://ufdc.ufl.edu/AA00029767

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Rao, Chetana Manohar, 1963-. “A Detailed investigation into the enzymatic specificity of porcine pepsin.” 1994. Thesis, University of Florida. Accessed August 23, 2019. http://ufdc.ufl.edu/AA00029767.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Rao, Chetana Manohar, 1963-. “A Detailed investigation into the enzymatic specificity of porcine pepsin.” 1994. Web. 23 Aug 2019.

Vancouver:

Rao, Chetana Manohar 1. A Detailed investigation into the enzymatic specificity of porcine pepsin. [Internet] [Thesis]. University of Florida; 1994. [cited 2019 Aug 23]. Available from: http://ufdc.ufl.edu/AA00029767.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Rao, Chetana Manohar 1. A Detailed investigation into the enzymatic specificity of porcine pepsin. [Thesis]. University of Florida; 1994. Available from: http://ufdc.ufl.edu/AA00029767

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


ETH Zürich

12. Serafimov, Jörg Michael. Mechanistic investigations of macrophomate synthase.

Degree: 2007, ETH Zürich

Subjects/Keywords: SYNTHASEN (ENZYME); BENZOESÄURE UND DERIVATE (AROMATISCHE CARBONSÄUREN); ENZYMREAKTION + ENZYMATISCHER REAKTIONSMECHANISMUS + ENZYMATISCHE KATALYSE (BIOCHEMIE); PERICYCLISCHE REAKTIONEN (ORGANISCHE CHEMIE); DIELS-ALDER-REAKTION + RETRO-DIELS-ALDER-REAKTION (CHEMISCHE REAKTIONEN); REAKTIONSMECHANISMEN + REAKTIVITÄT (CHEMISCHE KINETIK); STRUKTURAUFKLÄRUNG (ANALYTISCHE CHEMIE); SYNTHASES (ENZYMES); BENZOIC ACID AND DERIVATIVES (AROMATIC CARBOXYLIC ACIDS); ENZYMATIC REACTIONS + ENZYMATIC REACTION MECHANISM + ENZYMATIC CATALYSIS (BIOCHEMISTRY); PERICYCLIC REACTIONS (ORGANIC CHEMISTRY); DIELS-ALDER REACTION + RETRO DIELS-ALDER REACTIONS (CHEMICAL REACTIONS); REACTION MECHANISMS + REACTIVITY (CHEMICAL KINETICS); STRUCTURE DETERMINATION (ANALYTICAL CHEMISTRY); info:eu-repo/classification/ddc/540; Chemistry

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APA (6th Edition):

Serafimov, J. M. (2007). Mechanistic investigations of macrophomate synthase. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/149769

Chicago Manual of Style (16th Edition):

Serafimov, Jörg Michael. “Mechanistic investigations of macrophomate synthase.” 2007. Doctoral Dissertation, ETH Zürich. Accessed August 23, 2019. http://hdl.handle.net/20.500.11850/149769.

MLA Handbook (7th Edition):

Serafimov, Jörg Michael. “Mechanistic investigations of macrophomate synthase.” 2007. Web. 23 Aug 2019.

Vancouver:

Serafimov JM. Mechanistic investigations of macrophomate synthase. [Internet] [Doctoral dissertation]. ETH Zürich; 2007. [cited 2019 Aug 23]. Available from: http://hdl.handle.net/20.500.11850/149769.

Council of Science Editors:

Serafimov JM. Mechanistic investigations of macrophomate synthase. [Doctoral Dissertation]. ETH Zürich; 2007. Available from: http://hdl.handle.net/20.500.11850/149769


ETH Zürich

13. Finkelmann, Arndt R. Chemical reactivity of hydrogenases.

Degree: 2014, ETH Zürich

Subjects/Keywords: REACTION MECHANISMS + REACTIVITY (CHEMICAL KINETICS); DICHTEFUNKTIONALE (QUANTENCHEMIE U. QUANTENMECHANIK); WASSERSTOFFHERSTELLUNG (GASTECHNOLOGIE); HYDROGENASEN (ENZYME); HYDROGEN PRODUCTION (GAS TECHNOLOGY); REAKTIONSMECHANISMEN + REAKTIVITÄT (CHEMISCHE KINETIK); DENSITY FUNCTIONALS (QUANTUM CHEMISTRY AND QUANTUM MECHANICS); ENZYMREAKTION + ENZYMATISCHER REAKTIONSMECHANISMUS + ENZYMATISCHE KATALYSE (BIOCHEMIE); ENZYMATIC REACTIONS + ENZYMATIC REACTION MECHANISM + ENZYMATIC CATALYSIS (BIOCHEMISTRY); HYDROGENASES (ENZYMES); info:eu-repo/classification/ddc/540; info:eu-repo/classification/ddc/540; Chemistry; Chemistry

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APA (6th Edition):

Finkelmann, A. R. (2014). Chemical reactivity of hydrogenases. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/93022

Chicago Manual of Style (16th Edition):

Finkelmann, Arndt R. “Chemical reactivity of hydrogenases.” 2014. Doctoral Dissertation, ETH Zürich. Accessed August 23, 2019. http://hdl.handle.net/20.500.11850/93022.

MLA Handbook (7th Edition):

Finkelmann, Arndt R. “Chemical reactivity of hydrogenases.” 2014. Web. 23 Aug 2019.

Vancouver:

Finkelmann AR. Chemical reactivity of hydrogenases. [Internet] [Doctoral dissertation]. ETH Zürich; 2014. [cited 2019 Aug 23]. Available from: http://hdl.handle.net/20.500.11850/93022.

Council of Science Editors:

Finkelmann AR. Chemical reactivity of hydrogenases. [Doctoral Dissertation]. ETH Zürich; 2014. Available from: http://hdl.handle.net/20.500.11850/93022

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