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Diffusion-limited enzyme (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Diffusion-limited enzyme" in English language version.

refsWebsite
Global rank English rank
15nih.gov
4th place
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14doi.org
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3harvard.edu
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2worldcat.org
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2semanticscholar.org
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1jstor.org
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1arxiv.org
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1archives-ouvertes.fr
1,031st place
879th place

archives-ouvertes.fr

hal.archives-ouvertes.fr

arxiv.org

doi.org

  • Bar-Even, Arren; Noor, Elad; Savir, Yonatan; Liebermeister, Wolfram; Davidi, Dan; Tawfik, Dan S; Milo, Ron (2011). "The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters". Biochemistry. 50 (21): 4402–10. doi:10.1021/bi2002289. PMID 21506553.
  • Alberty, Robert A.; Hammes, Gordon G. (1958). "Application of the Theory of Diffusion-controlled Reactions to Enzyme Kinetics". Journal of Physical Chemistry. 62 (2): 154–9. doi:10.1021/j150560a005.
  • Eigen, Manfred; Hammes, Gordon G. (2006). "Elementary Steps in Enzyme Reactions (as Studied by Relaxation Spectrometry)". In Nord, F. F. (ed.). Advances in Enzymology and Related Areas of Molecular Biology. Vol. 25. pp. 1–38. doi:10.1002/9780470122709.ch1. ISBN 978-0-470-12270-9. OCLC 777630506. PMID 14149678. {{cite book}}: |journal= ignored (help)
  • Koenig, Seymour H.; Brown, Rodney D. (1972). "H2CO3 as Substrate for Carbonic Anhydrase in the Dehydration of HCO3−". Proceedings of the National Academy of Sciences of the United States of America. 69 (9): 2422–5. Bibcode:1972PNAS...69.2422K. doi:10.1073/pnas.69.9.2422. JSTOR 61783. PMC 426955. PMID 4627028.
  • Riggs, Arthur D; Bourgeois, Suzanne; Cohn, Melvin (1970). "The lac repressor-operator interaction". Journal of Molecular Biology. 53 (3): 401–17. doi:10.1016/0022-2836(70)90074-4. PMID 4924006.
  • Kirschner, Kasper; Gallego, Ernesto; Schuster, Inge; Goodall, David (1971). "Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase". Journal of Molecular Biology. 58 (1): 29–50. doi:10.1016/0022-2836(71)90230-0. PMID 4326080.
  • Chou, Kuo Chen; Zhou, Guo Ping (1982). "Role of the protein outside active site on the diffusion-controlled reaction of enzymes". Journal of the American Chemical Society. 104 (5): 1409–1413. doi:10.1021/ja00369a043.
  • Payens, T.A.J (1983). "Why are enzymes so large?". Trends in Biochemical Sciences. 8 (2): 46. doi:10.1016/0968-0004(83)90382-1.
  • Zhou, Guozhi; Wong, Ming-Tat; Zhou, Guo-Qiang (1983). "Diffusion-controlled reactions of enzymes". Biophysical Chemistry. 18 (2): 125–32. doi:10.1016/0301-4622(83)85006-6. PMID 6626685.
  • Zhou, Guo-Qiang; Zhong, Wei-Zhu (1982). "Diffusion-Controlled Reactions of Enzymes". European Journal of Biochemistry. 128 (2–3): 383–7. doi:10.1111/j.1432-1033.1982.tb06976.x. PMID 7151785.
  • Garcia-Viloca, M; Gao, Jiali; Karplus, Martin; Truhlar, Donald G (2004). "How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations". Science. 303 (5655): 186–95. Bibcode:2004Sci...303..186G. doi:10.1126/science.1088172. PMID 14716003. S2CID 17498715.
  • Olsson, Mats H. M.; Siegbahn, Per E. M.; Warshel, Arieh (2004). "Simulations of the Large Kinetic Isotope Effect and the Temperature Dependence of the Hydrogen Atom Transfer in Lipoxygenase". Journal of the American Chemical Society. 126 (9): 2820–8. doi:10.1021/ja037233l. PMID 14995199.
  • Jevtic, S; Anders, J (2017). "A qualitative quantum rate model for hydrogen transfer in soybean lipoxygenase". The Journal of Chemical Physics. 147 (11): 114108. arXiv:1612.03773. Bibcode:2017JChPh.147k4108J. doi:10.1063/1.4998941. PMID 28938801. S2CID 11202267.
  • Domnik, Lilith; Merrouch, Meriem; Goetzl, Sebastian; Jeoung, Jae-Hun; Léger, Christophe; Dementin, Sébastien; Fourmond, Vincent; Dobbek, Holger (2017-11-27). "CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2" (PDF). Angewandte Chemie International Edition. 56 (48): 15466–15469. doi:10.1002/anie.201709261. ISSN 1521-3773. PMID 29024326.

harvard.edu

ui.adsabs.harvard.edu

jstor.org

nih.gov

pubmed.ncbi.nlm.nih.gov

  • Bar-Even, Arren; Noor, Elad; Savir, Yonatan; Liebermeister, Wolfram; Davidi, Dan; Tawfik, Dan S; Milo, Ron (2011). "The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters". Biochemistry. 50 (21): 4402–10. doi:10.1021/bi2002289. PMID 21506553.
  • Eigen, Manfred; Hammes, Gordon G. (2006). "Elementary Steps in Enzyme Reactions (as Studied by Relaxation Spectrometry)". In Nord, F. F. (ed.). Advances in Enzymology and Related Areas of Molecular Biology. Vol. 25. pp. 1–38. doi:10.1002/9780470122709.ch1. ISBN 978-0-470-12270-9. OCLC 777630506. PMID 14149678. {{cite book}}: |journal= ignored (help)
  • Koenig, Seymour H.; Brown, Rodney D. (1972). "H2CO3 as Substrate for Carbonic Anhydrase in the Dehydration of HCO3−". Proceedings of the National Academy of Sciences of the United States of America. 69 (9): 2422–5. Bibcode:1972PNAS...69.2422K. doi:10.1073/pnas.69.9.2422. JSTOR 61783. PMC 426955. PMID 4627028.
  • Chou, Kuo-Chen; Jiang, Shou-Ping (1974). "Studies on the rate of diffusion-controlled reactions of enzymes. Spatial factor and force field factor". Scientia Sinica. 27 (5): 664–80. PMID 4219062.
  • Chou, Kuo-Chen (1976). "The kinetics of the combination reaction between enzyme and substrate". Scientia Sinica. 19 (4): 505–28. PMID 824728.
  • Li, TT; Chou, KC (1976). "The quantitative relations between diffusion-controlled reaction rate and characteristic parameters in enzyme-substrate reaction systems. I. Neutral substrates". Scientia Sinica. 19 (1): 117–36. PMID 1273571.
  • Riggs, Arthur D; Bourgeois, Suzanne; Cohn, Melvin (1970). "The lac repressor-operator interaction". Journal of Molecular Biology. 53 (3): 401–17. doi:10.1016/0022-2836(70)90074-4. PMID 4924006.
  • Kirschner, Kasper; Gallego, Ernesto; Schuster, Inge; Goodall, David (1971). "Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase". Journal of Molecular Biology. 58 (1): 29–50. doi:10.1016/0022-2836(71)90230-0. PMID 4326080.
  • Zhou, Guozhi; Wong, Ming-Tat; Zhou, Guo-Qiang (1983). "Diffusion-controlled reactions of enzymes". Biophysical Chemistry. 18 (2): 125–32. doi:10.1016/0301-4622(83)85006-6. PMID 6626685.
  • Zhou, Guo-Qiang; Zhong, Wei-Zhu (1982). "Diffusion-Controlled Reactions of Enzymes". European Journal of Biochemistry. 128 (2–3): 383–7. doi:10.1111/j.1432-1033.1982.tb06976.x. PMID 7151785.
  • Garcia-Viloca, M; Gao, Jiali; Karplus, Martin; Truhlar, Donald G (2004). "How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations". Science. 303 (5655): 186–95. Bibcode:2004Sci...303..186G. doi:10.1126/science.1088172. PMID 14716003. S2CID 17498715.
  • Olsson, Mats H. M.; Siegbahn, Per E. M.; Warshel, Arieh (2004). "Simulations of the Large Kinetic Isotope Effect and the Temperature Dependence of the Hydrogen Atom Transfer in Lipoxygenase". Journal of the American Chemical Society. 126 (9): 2820–8. doi:10.1021/ja037233l. PMID 14995199.
  • Jevtic, S; Anders, J (2017). "A qualitative quantum rate model for hydrogen transfer in soybean lipoxygenase". The Journal of Chemical Physics. 147 (11): 114108. arXiv:1612.03773. Bibcode:2017JChPh.147k4108J. doi:10.1063/1.4998941. PMID 28938801. S2CID 11202267.
  • Domnik, Lilith; Merrouch, Meriem; Goetzl, Sebastian; Jeoung, Jae-Hun; Léger, Christophe; Dementin, Sébastien; Fourmond, Vincent; Dobbek, Holger (2017-11-27). "CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2" (PDF). Angewandte Chemie International Edition. 56 (48): 15466–15469. doi:10.1002/anie.201709261. ISSN 1521-3773. PMID 29024326.

ncbi.nlm.nih.gov

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