John E. Walker

John E. Walker is a British biochemist who shared the 1997 Nobel Prize in Chemistry for revealing how ATP synthase produces ATP.

Paul D. Boyer: An American biochemist who shared the 1997 Nobel Prize in Chemistry for explaining ATP synthase’s catalytic mechanism. Boyer independently developed the binding-change model that Walker’s structural work helped establish.
ATP synthase: A membrane enzyme that uses an ion gradient to synthesize ATP from ADP and phosphate. This is the enzyme whose structure and catalytic action Walker investigated.
Protein sequencing: The determination of the amino-acid order in a protein or one of its subunits. Walker’s early ATP synthase research established subunit sequences before structural analysis.
Chemiosmotic theory: The theory that ion gradients across membranes drive cellular energy conversion. Walker’s work identified the molecular machine that uses the proton gradient predicted by this theory.
Jens C. Skou: A Danish physician and biochemist who discovered the sodium-potassium pump and shared the 1997 Nobel Prize in Chemistry. Skou shared Walker’s Nobel Prize for a distinct discovery about membrane transport.
Binding-change mechanism: A model in which ATP synthase’s catalytic sites cycle through states that bind substrates, form ATP, and release it. Walker’s structures supported the rotating catalytic states described by this model.
X-ray crystallography: A method for determining molecular structures by analyzing how crystals diffract X-rays. Walker’s team used crystallography to resolve ATP synthase’s catalytic architecture.
Molecular motor: A molecular machine that converts chemical energy into directed mechanical motion or vice versa. ATP synthase became a landmark example of a motor operating at molecular scale.
Andrew Leslie: A British crystallographer who collaborated with John Walker on determining the structure of ATP synthase’s catalytic subunit. Leslie’s crystallographic collaboration helped reveal the enzyme’s molecular architecture.
F1 ATPase: The soluble catalytic portion of ATP synthase that can hydrolyze ATP and contains three catalytic beta subunits. Walker’s structural studies focused on this catalytic portion of the enzyme.

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Jens Christian SkouRelated: Walker shared the prize with Skou and Boyer for work on ATP synthase.