J. B. S. Haldane

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    As commonly done, we will omit the spaces between the initials when we refer to J. B. S. Haldane in this article.

Referred to by most as J. B. S. Haldane (or J.B.S. Haldane), sometimes 'Jack', the initials stand for John Burdon Sanderson ('Burdon Sanderson' from his maternal line), born in Oxford, England, in 1892, his father an accomplished and honored (respiratory) physiologist, John Scott Haldane (J. S. Haldane),[1] with whom J.B.S. worked as his laboratory assistant during childhood.[2][3] Educated at Eaton (equivalent to an American high school)[4] and Oxford University, receiving his undergraduate degree in 1914 — in classics, philosophy and ancient history, graduating with honors — served in combat in World War I, and later teaching and doing research at Oxford (1919, elected Fellow in physiology), Cambridge (1922-1932), and University College London (1933, appointed professor of genetics; 1937, appointed Weldon Chair in Biometry), and for a short time at the University of California at Berkeley. In 1932 J.B.S. Haldane published The Causes of Evolution, a founding document in the modern evolutionary synthesis of population genetics, reflecting the interest he developed in college in biology, genetics and applying mathematics to questions in biology and genetics.[2]

This article will give a summary of J.B.S. Haldane's life and thinking, his contributions to science and to the popularization of science, his impact on his times, and his vision of the future. One science historian, Mark B. Adams, sets the task:

J.B.S. Haldane (1892-1964) is one of the most fascinating, perplexing and troublesome figures in the history of science. That he was a major biologist of his time goes without saying, but attempts at further scientific classification are futile: there is hardly a field of modern biology in whose history he does not deserve at least some mention. And, beyond biology proper, Haldane had yet other personae that at times seemed no less central to his career. Any attempt to come to terms with his life and work must face the dual challenge of his extraordinary multiformity and his utter singularity. [5]

Haldane's youth

As a child J.B.S. Haldane learned much of his father's 'trade', human physiology, essentially as an non-indentured apprentice. He states in his "An Autobiography in Brief":

At the age of eight or so I was allowed to take down numbers which I called out when reading the burette of a gas-analysis apparatus and later to calculate from these numbers the amounts of various gases in a sample. After this I was promoted to making up simple mixtures for his use and, still later, to cleaning apparatus. Before I was fourteen, he had taken me down a number of mines, and I had spent some time under water both in a submarine and in a diving dress. He had also used me as the subject in many experiments. In fact I spent a good deal of my holidays from school in learning my father's trade…After I was twelve, he discussed with me all his research before publication, and sometimes tried out a lecture course on me before delivering it to students.[3]

His father also introduced him to genetics early on, at age eight years, when he accompanied his father to hear a lecture by the geneticist, A. D. Darbishire, about the rediscovery of Gregor Mendel's laws of heredity.[6] Not surprisingly, the younger Haldane pursued the science of genetics throughout his life.

By age fourteen years he had apparently learned about gases and human respiratory physiology, learned mathematical applications for interpreting experimental data, and from discussions with his father, learned about presenting research results for publication, and about developing lecture courses. (For more on J.B.S. Haldane's father's life and scientific work, see[1])  J.B.S. Haldane had a head start in science and scientific thinking, leading him in school to complement his studyies Latin and Greek with studies of physics, chemistry and biology — and history.[3].

Through his study of chemistry, he reportedly had learned about advances in chemical knowledge that helped his father and colleague, C. G. Douglas, in their research. His first scientific paper, at age seventeen years (1909), co-authored with his father and C. G. Douglas, was read to the Physiological Society, likely what appeared in the Journal of Physiology in 1912, as Douglas CG, Haldane JS, Haldane JB. (1912) The laws of combination of haemoglobin with carbon monoxide and oxygen. J. Physiol 44:275-304.[7]  It reflected physiology at the mathematical and chemical level. J.B.S. Haldane had achieved credentials as a scientist with sophisticated mathematical ability by age twenty years, and he followed up in the years ahead with mathematical perspectives applied in enzymology and population genetics (vide infra).

Scientific contributions

In 1992, 100 years after Haldane's birth, the Science Museum in London hosted a centenary celebration in honor of Haldane. Sahotra Sarkar briefly summarized Haldane's scientific contributions as follows:[6]

What is most remarkable about Haldane is the extent to which he contributed to a wide and disparate variety of fields.

  • He was one of the founders of theoretical population genetics, probably his greatest single achievement.
  • He was responsible for what still is the standard model of enzyme kinetics. [kinetics===]
  • He was one of the first to suggest a connection between genes and enzymes.
  • He initiated a program of research that led to the formulation of chemical genetics, the precursor of biochemical genetics, in the 1930s.
  • He proposed the heterotrophic model for the origin of life independent of A. I. Oparin, and only a few years later.
  • He was the first to introduce the concepts of genetic load and the cost of natural selection.
  • In 1945, he proposed a new and, at that time, plausible though controversial model for the origin of the solar system. [reformatted as bullets]

     Enzyme kinetics

Early on (1925), at Cambridge University, Haldane applied his evidenced passion for mathematical analysis of biological chemistry to the field of enzymology. Enzymologists study the behavior of enzymes, the protein catalysts that accelerate biochemical reactions in living cells without themselves getting consumed in the reactions. Among other studies, enzymologists perform schematic and mathematical modeling of the many different kinds of biochemical reactions catalyzed by enzymes. With a colleague, George E. Briggs, Haldane presented a theoretical analysis that could account for quantitative measurements of the rates of many of such reactions, using a different reaction equation and a more generally valid assumption about the nature of enzyme catalyzed reaction than the earlier model presented by Michaelis and Menten.[8] The Briggs-Haldane analysis remains in the mainstream of enzymatic reaction ‘kinetics’, and has set a foundation for, and stimulated, the further developments in that field up to the 21st century.[9][10]

For further description of the Briggs-Haldane modification of the Michaelis-Menten equation see the original publication,[8] or online, see Palmer.[11]

Later (1930) he wrote a book entitled Enzymes in which he further elaborated on the Briggs-Haldane analysis, mathematically modeled more complex enzyme catalyzed reactions, speculated on the details of the molecular interactions, anticipating the so-called strain theory of enzyme catalysis.[12] For more on the strain theory of enzyme catalysis, see for example,[13] and the references therein.

References

Citations and notes

  1. 1.0 1.1 Editors. (1936) The Late Professor J. S. Haldane, C.H., M.D., F.R.S. Can Med Assoc J. August; 35(2): 197–198.
  2. 2.0 2.1 Bookrags Collection of Sources of Biographical Information on J. B. S. Haldane
  3. 3.0 3.1 3.2 Haldane JBS. (1966) An autobiography in brief. Perspectives in Biology and Medicine Summer. (The editors noted: "Professor Haldane died December 1, 1964. This article is reprinted with the kind permission of the illustrated Weekly of India, Bombay.") Cite error: Invalid <ref> tag; name "haldaneautobio" defined multiple times with different content
  4. Note: Among Eaton's students who subsequently entered scientific fields: Robert Boyle, John Herschel, Julian Huxley, John William Strutt (Lord Rayleigh), Stephen Wolfram. Famous Old Etonians
  5. Adams MB. (2000) Last Judgment: The Visionary Biology of J. B. S. Haldane. J Hist Biol. 33:457-491
  6. 6.0 6.1 Sarkar S. (1992) A centenary reassessment of J. B. S. Haldane, 1892-1964. (biologist). Bioscience 42:777-779
  7. Douglas CG, Haldane JS, Haldane JB. (1912) The laws of combination of haemoglobin with carbon monoxide and oxygen. J. Physiol 44:275-304. Free Full-Text
  8. 8.0 8.1 Briggs GE, Haldane JBS. (1925) A note on the kinetics of enzyme reactions. Biochem J 19:338-339
    • They end the paper: “It may be remarked that with this modification of their [earlier] theory, Michaelis and Menten's analysis of the effects of the products of the reaction, or other substances which combine with the enzyme, still holds good.”
  9. Tzafriri AR, Edelman ER. (2004) The total quasi-steady-state approximation is valid for reversible enzyme kinetics. Journal of Theoretical Biology 226 (3):303-313]
  10. Pedersena MG, Bersani AM, and Bersani E. (2007) The total quasi-steady-state approximation for fully competitive enzyme reactions. Bull.Math.Biol. 69 (1):433-457 PMID 16850351
  11. Palmer T. (2001) Enzymes: Biochemistry, Biotechnology, Clinical Chemistry, “The Briggs-Haldane modification of the Michaelis-Menten equation”, pages 109-111 Horwood Publishing, ISBN 1898563780
  12. Haldane JBS. (1930) Enzymes Longmans, Green and Co.
  13. Yin J, Andryski SE, Beuscher AE IV, Stevens RC, Schultz PG. (2003) [http://dx.doi.org/10.1073/pnas.0235873100 Structural evidence for substrate strain in antibody catalysis. PNAS 100:856-861
    • Note: From the Introduction: "Modern theories of biological catalysis date from Haldane's theory of strain: 'using Fischer's lock and key simile, the key does not fit the lock perfectly but exercises a certain strain on it' (citation to Haldane's Enzymes)...the notion that enzymes use binding energy to strain or distort substrates is a fundamental theory of enzyme catalysis (citation...")