María Luz Cárdenas
María Luz Cárdenas | |
---|---|
María Luz Cárdenas in Tenerife, 2008 | |
Born | María de la Luz Ilze Palmira Antonia Cárdenas Cerda 7 June 1944 |
Education | University of Chile |
Known for | Discvery of kinetic cooperativity in a monomeric enzyme |
Spouse | Athel Cornish-Bowden |
Awards | Tito Ureta Prize, Chilean Society of Biochemistry and Molecular Biology |
Scientific career | |
Fields | Enzyme kinetics, nature of life |
Institutions | University of Chile; Birmingham University; Aix-Marseille University; CNRS, Marseille |
Thesis | Glucoquinasa, una enzima monomérica con cinética cooperativa (1982) |
Academic advisors | Hermann 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
- ^ a b c d Reyes-Corral, Marta, ed. (2024). Women's Careers in Science (PDF). FEBS (Federation of European Biochemical Societies).
- ^ a b "María Luz Cárdenas, Doctor en Ciencias". Chemistry Tree. 2017.
- ^ "People". Bioénergétique et Ingénierie des Protéines (BIP, CNRS). 2025.
- ^ a b Cárdenas, María Luz (1995). “Glucokinase”: Its Regulation and Role in Liver Metabolism. Springer. ISBN 3-540-59285-7.
- ^ "Gluconasa, una enzima monomérica con cinética cooperativa [Glucoquinasa misspelt]". Repositorio Académico de la Universidad de Chile. 2020.
- ^ 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.
- ^ 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.
- ^ 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. PMC 1164031.
- ^ 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. PMC 1264826. PMID 4223117.
- ^ 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. PMC 1270296. PMID 6029595.
- ^ Monod, J; Wyman, J; Changeux, J–P (1965). "On the nature of allosteric transitions: A plausible model". Journal of Molecular Biology. 12: 88–118. doi:10.1016/S0022-2836(65)80285-6. PMID 14343300.
- ^ 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.
- ^ 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.
- ^ 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. PMC 1144187.
- ^ 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.
- ^ 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.
- ^ 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. hdl:10533/130549.
- ^ 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.
- ^ Cornish-Bowden, A; Cárdenas, M L (2017). "Life before LUCA". J. Theor. Biol. 434: 68–74. doi:10.1016/j.jtbi.2017.05.023.
- ^ "Miembros Correspondientes extranjeros". Academia Chilena de Ciencias, Instituto de Chile. 2002.
- ^ "María de la Luz Cárdenas Cerda Premio Dr. Tito Ureta 2016". Chilean Society of Biochemistry and Molecular Biology.
- ^ "Socios de Honor". Sociedad Espanola de Bioquímica y la Biología Molecular. 2023.
- ^ "Groupes thématiques". Société Française de Biochimie et Biologie Moléculaire.