Biography:María Luz Cárdenas

From HandWiki
María Luz Cárdenas
María Luz Cárdenas in Tenerife, 2008
Born
María de la Luz Ilze Palmira Antonia Cárdenas Cerda

(1944-06-07) 7 June 1944 (age 82)
Santiago, Chile
EducationUniversity of Chile
Known forDiscvery of kinetic cooperativity in a monomeric enzyme
Spouse(s)Athel Cornish-Bowden
AwardsTito Ureta Prize, Chilean Society of Biochemistry and Molecular Biology
Scientific career
FieldsEnzyme kinetics, nature of life
InstitutionsUniversity of Chile; Birmingham University; Aix-Marseille University; CNRS, Marseille
ThesisGlucoquinasa, una enzima monomérica con cinética cooperativa (1982)
Academic advisorsHermann Niemeyer

María Luz Cárdenas Cerda (born 7 June 1944) is a French biochemist of Chilean origin. She is known for studies of mammalian hexokinases and for developing understanding of the nature of life.

Personal life

María Luz Cárdenas was born on 7 June 1944 in Santiago, Chile, the daughter of Palmira Rebeca Cerda Fuenzalida and Oscar Guillermo Cárdenas Ubilla, and she spent her early life and education in Santiago.[1] After four years in Birmingham, United Kingdom,[2] she moved to Marseille, France in 1987 as a researcher in the CNRS, and remained there for the rest of her working life.[2][3]

She married Athel Cornish-Bowden in 1982 and had one daughter.[4]: Acknowledgements 

Education

Cárdenas studied biochemistry at the University of Chile, and worked for her doctoral thesis with Hermann Niemeyer.[1]

Career

In Chile in the 1980s and earlier there were no grants for post-graduate students, and so it was necessary for Cárdenas to work as a teaching assistant and lecturer at the University of Chile at the same time as working towards her doctorate under Hermann Niemeyer, with a thesis entitled Glucoquinasa, una enzima monomérica con cinética cooperativa[5] (Glucokinase, a monomeric enzyme with kinetic cooperativity).

Research

Hexokinase D

Cárdenas's doctoral research led to a major discovery, that rat-liver hexokinase D (often called “glucokinase”) was a monomeric enzyme[6] that displayed positive cooperativity,[7] later confirmed by others.[8] Although kinetic models of cooperativity had been proposed (for example by Ferdinand[9] and by Rabin[10]) these were not widely believed to have practical importance, and cooperativity was usually assumed to require binding equilibrium and interactions between multiple binding sites. Hexokinase D was thus the first enzyme for which the cooperativity could not be explained in terms of the best known models.[11][12] Cárdenas and co-workers suggested that the cooperativity could be explained by a slow-transition model.[13]

The name “glucokinase” for hexokinase D is now virtually universal in the literature, and there is little likelihood of changing that. However, it is important to realize that it is a misleading name, because it implies that hexokinase D is more specific for glucose than the other mammalian hexokinases, but that is not the case, as it accepts fructose as a good substrate.[14]

Although the monomeric cooperativity exhibited by hexokinase D proved to be rare, it was not the only example.[15]

Cárdenas's book “Glucokinase”: Its Regulation and Role in Liver Metabolism collects a large amount of information about the enzyme, not only about its kinetics and cooperativity, but its physiological importance in regulating glucose uptake by the liver, and genetic aspects.[4] Her work on hexokinase D inevitably led to study of the other mammalian hexokinase isoenzymes and their evolution, as set out in her review.[16]

Nature of life

In the last 20 years of her career, Cárdenas's interest turned to the nature of life,[17] self-organization,[18] and LUCA (the last universal common ancestor).[19]

Honours

In 1993 Cárdenas was appointed to the honorary chair "Hermann Niemeyer F." at the Faculty of Sciences of the University de Chile.[1] In 2002 she was elected corresponding member of the Chilean Academy of Sciences.[20] In 2016 she was awarded the Tito Ureta Prize of the Chilean Society of Biochemistry and Molecular Biology.[21] In 2023 she was elected Honorary Member of the Spanish Society of Biochemistry and Molecular Biology.[22] In 2024 the French Society of Biochemistry and Molecular Biology nominated her as one of 36 women scientists celebrated by FEBS,[1] recognizing her creation as a thematic group of the Society the Association pour les Femmes en Sciences et Ingénierie as a way of contributing to the visibility of women scientists,[23]

References

  1. ↑ 1.0 1.1 1.2 1.3 Reyes-Corral, Marta, ed (2024). Women's Careers in Science. FEBS (Federation of European Biochemical Societies). https://www.febs.org\wp-content/uploads/2024/11/FEBS-Womens-Careers-in-Science-v2024.11.29.pdf. 
  2. ↑ 2.0 2.1 "María Luz Cárdenas, Doctor en Ciencias". Chemistry Tree. 2017. https://academictree.org/chemistry/peopleinfo.php?pid=735835. 
  3. ↑ "People". Bioénergétique et Ingénierie des Protéines (BIP, CNRS). 2025. https://bip.cnrs.fr/groups/bip01/people/. 
  4. ↑ 4.0 4.1 Cárdenas, María Luz (1995). "Glucokinase": Its Regulation and Role in Liver Metabolism. Springer. ISBN 3-540-59285-7. 
  5. ↑ "Gluconasa, una enzima monomérica con cinética cooperativa [Glucoquinasa misspelt"]. Repositorio Académico de la Universidad de Chile. 2020. https://repositorio.uchile.cl/handle/2250/194206. 
  6. ↑ Niemeyer, H; Cárdenas, María Luz; Rabajille, Eliana (1978). "Maintenance of the monomeric structure of glucokinase under reacting conditions". Arch. Biochem. Biophys. 190 (1): 142–148. doi:10.1016/0003-9861(78)90261-8. PMID 708068. https://repositorio.uchile.cl/handle/2250/154128. 
  7. ↑ Niemeyer, H; Cárdenas, M L; Rabajille, E; Ureta, T; Clark-Turri, L; Peñaranda, J (1975). "Sigmoidal kinetics of glucokinase". Enzyme 20 (6): 321–333. doi:10.1159/000458957. PMID 1193069. 
  8. ↑ Storer, A C; Cornish-Bowden, A (1976). "Kinetics of rat liver glucokinase. Co-operative interactions with glucose at physiologically significant concentrations". Biochem. J. 159 (1): 7–14. doi:10.1042/bj1590007. PMID 999645. 
  9. ↑ Ferdinand, W (1966). "The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinase". Biochem. J. 98 (1): 278–283. doi:10.1042/bj0980278. PMID 4223117. 
  10. ↑ Rabin, B R (1967). "Co-operative effects in enzyme catalysis: a possible kinetic model based on substrate-induced conformation isomerization". Biochem. J. 102 (2): 22C–23C. doi:10.1042/bj1020022c. PMID 6029595. 
  11. ↑ Monod, J; Wyman, J; Changeux, J–P (1965). "On the nature of allosteric transitions: A plausible model". Journal of Molecular Biology 12 (1): 88–118. doi:10.1016/S0022-2836(65)80285-6. PMID 14343300. Bibcode: 1965JMBio..12...88M. 
  12. ↑ Koshland, D. E.; Némethy, G.; Filmer, D. (1966). "Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits". Biochemistry 5 (1): 365–385. doi:10.1021/bi00865a047. PMID 5938952. Bibcode: 1966Bioc....5..365K. 
  13. ↑ Niemeyer, H; Cárdenas, M L; Rabajille, E (1984). "Suppression of kinetic cooperativity of hexokinase D (glucokinase) by competitive inhibitors. A Slow transition model". Eur. J. Biochem. 145 (1): 163–171. doi:10.1111/j.1432-1033.1984.tb08536.x. 
  14. ↑ Cárdenas, M L; Rabajille, E; Niemeyer, H (1984). "Fructose is a good substrate for rat liver 'glucokinase' (hexokinase D)". Biochem. J. 222 (2): 363–370. doi:10.1042/bj2220363. PMID 6477520. 
  15. ↑ Cornish-Bowden, A; Cárdenas, M L (1987). "Co-operativity in monomeric enzymes". J. Theor. Biol. 124 (1): 1–23. doi:10.1016/S0022-5193(87)80248-5. PMID 3309473. Bibcode: 1987JThBi.124....1C. 
  16. ↑ Cárdenas, M L; Cornish-Bowden, A; Ureta, T (1998). "Evolution and regulatory role of the hexokinases". Biochim. Biophys. Acta 1401 (3): 242–264. doi:10.1016/S0167-4889(97)00150-X. PMID 9540816. 
  17. ↑ Letelier, J C; Cárdenas, M L; Cornish-Bowden, A (2011). "From L'Homme Machine to metabolic closure: Steps towards understanding life". J. Theor. Biol. 286: 100–113. doi:10.1016/j.jtbi.2011.06.033. PMID 21763318. Bibcode: 2011JThBi.286..100L. 
  18. ↑ Letelier, J C; Soto-Andrade, J; Guíñez Abarzúa, F; Cornish-Bowden, A; Cárdenas, M L (2006). "Organizational invariance and metabolic closure: Analysis in terms of (M, R ) systems". J. Theor. Biol. 238 (5): 949–961. doi:10.1016/j.jtbi.2005.07.007. PMID 16122760. Bibcode: 2006JThBi.238..949L. 
  19. ↑ Cornish-Bowden, A; Cárdenas, M L (2017). "Life before LUCA". J. Theor. Biol. 434: 68–74. doi:10.1016/j.jtbi.2017.05.023. PMID 28536033. Bibcode: 2017JThBi.434...68C. 
  20. ↑ "Miembros Correspondientes extranjeros". Academia Chilena de Ciencias, Instituto de Chile. 2002. https://www.academiadeciencias.cl/miembros-correspondientes-extranjeros/. 
  21. ↑ "María de la Luz Cárdenas Cerda Premio Dr. Tito Ureta 2016". Chilean Society of Biochemistry and Molecular Biology. https://www.sbbmch.cl/maria-de-la-luz-cardenas-cerda-premio-dr-tito-ureta-2016/. 
  22. ↑ "Socios de Honor". Sociedad Espanola de Bioquímica y la Biología Molecular. 2023. https://sebbm.es/socios-de-honor/. 
  23. ↑ "Groupes thématiques". Société Française de Biochimie et Biologie Moléculaire. https://www.sfbbm.fr/index.php?option=com_content&view=category&id=54&Itemid=169&lang=fr. 



Retrieved from "https://handwiki.org/wiki/index.php?title=Biography:María_Luz_Cárdenas&oldid=4222617"