JOHN E. WALKER

JOHN E. WALKER

1997 Nobel Laureate in Chemistry "for elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP)"

Background
Born: 1941
Place of Birth: Halifax, Great Britain
Residence: Great Britain
Education: Received M.A. and Dr.Phil. at Oxford University, Great Britain
Affiliation: Medical Research Council Laboratory of Molecular Biology (Cambridge, UK)

In full John Ernest Walker British chemist who was corecipient, with Paul D. Boyer, of the Nobel Prize for Chemistry in 1997 for their explanation of the enzymatic process that creates adenosine triphosphate (ATP).

After receiving his doctorate from the University of Oxford in 1969, Walker undertook research projects at universities in the United States and Paris. His award-winning work
was conducted at the University of Cambridge in the Medical Research Council Laboratory of Molecular Biology, which he joined in 1974, becoming senior scientist in 1982.

Walker’s early research in the mid-1970s analyzed the sequences of the proteins from the bacteriophage G4 and from mitochondria. This led to the discovery of triple over-lapping genes in G4 (with D. Shaw and B.G. Barrell) and to the discovery that subunits I and II of cytochrome c oxidase were encoded in the DNA in mitochondria. He also helped to uncover the modified genetic code in mitochondria.During the work on mitochondria, he developed an interest in the enzyme complexes in the inner membrane of the organelle that carry out oxidative phosphorylation, in the early 1980s Walker began studying ATP synthase—the central energy-producing molecule in most life-forms—which aides in the synthesis of ATP, the carrier of chemical energy. Focusing on the chemical and structural composition of the enzyme, he determined the sequence of amino acids that make up the synthase's protein units. In the 1990s, working with X-ray crystallographers, Walker clarified the three-dimensional structure of the enzyme. His work supported Boyer's “binding change mechanism,” which explained the unusual way in which the enzyme functions. Walker's findings offer insight into the way life-forms produce energy.

He also received a Knighthood in 1999 and was named an honorary member of the British Physical Society in 2000.

Edited by: minhaz [minhaz@jaist.ac.jp]