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SUMMARY:HONORARY FELLOWS LECTURE - The Fuel of Life - Professor Sir John  
 E Walker FRS FMedSci\,Nobel Laureate in Chemistry\,  Medical Research Coun
 cil\, Mitochondrial Biology Unit 
DTSTART:20190206T180000Z
DTEND:20190206T190000Z
UID:TALK115807@talks.cam.ac.uk
CONTACT:Beverley Larner
DESCRIPTION:The lecture will be devoted to how the biological world suppli
 es itself with energy\, and what medical consequences ensue when the energ
 y supply chain in our bodies is damaged or defective\, and how we can put 
 our knowledge of how ATP is made to benefit mankind. We derive our energy 
 from sunlight\, via photosynthesis in green plants\, providing high energy
  components in the foods that we eat. We harvest that energy by “burning
 ” (oxidising) the high energy components\, releasing cellular energy in 
 a controlled way to generate the fuel of life\, in the form of the molecul
 e adenosine triphosphate (or ATP for short). The key steps in this process
  take place in the mitochondria inside the cells that make up our tissues.
  They serve as biological “power stations” containing millions of tiny
  molecular turbines\, the ATP synthase\, that rotate like man-made turbine
 s\, churning out the cellular fuel in large quantities\, which is then del
 ivered to all parts of our bodies to provide the energy to make them funct
 ion. Each of us makes and expends about 60 kg of this fuel every day of ou
 r lives. The ATP synthases consist of two rotary motors linked by a stator
  and a flexible rotor. Rotation of the membrane bound rotor is driven by t
 he proton motive force\, itself generated by oxidative metabolism (or by p
 hotosynthesis in green plants). A unique direction of rotation ensures tha
 t ATP is made from ADP and phosphate in the globular catalytic domain. How
 ever\, during anoxia\, ATP made by glycolysis serves as the source of ener
 gy and is hydrolysed in the catalytic domain. Then the rotor turns in the 
 opposite sense and protons are pumped outwards through the membrane domain
 \, and away from the catalytic domain. However\, for reasons yet to be unc
 overed some eubacterial ATP synthases\, which in many respects resemble th
 e ATP synthases in metazoans\, are unable to carry out this hydrolytic rea
 ction. \n\nWhy this is so\, is of great practical interest today\, as the 
 ATP synthase in Mycobacterium tuberculosis is a validated drug target for 
 the treatment of tuberculosis. In 2011\, 1.4 million people died from tube
 rculosis\, and Mycobacterium tuberculosis is now the second greatest kille
 r of mankind by a single infectious agent\, surpassed only by HIV/AIDS. A 
 further 7.3 million have been diagnosed with the active form of the diseas
 e\, and a third of the world’s population\, currently 7.2 billion people
 \, has been estimated to have a latent TB infection\, and to be at risk of
  progressing to the active disease. Today\, multi-drug resistant tuberculo
 sis\, extensively drug-resistant tuberculosis\, and totally resistant tube
 rculosis add to the difficulties of treating the disease. In 2015\, multid
 rug-resistant TB strains of M. tuberculosis caused an estimated 480\,000 n
 ew cases of TB and 250\,000 deaths. The differences between human ATP synt
 hases and those in bacterial pathogens can be exploited in the fight again
 st bacterial resistance to antibiotics.\n\nThe origins and propagation of 
 life on earth depended upon developing an ability to generate ATP\, and so
  I will end by discussing the question about how such a complex machine wa
 s put together early in evolution. Clues are to found in the process of ho
 w the modern ATP synthase is assembled.\n
LOCATION:Bristol-Myers Squibb Lecture Theatre\, Department of Chemistry
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