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Paul D. Boyer a 1997 Nobel Prize winner, recently died. He was 99 years old.
Among other things, he did important work on one of the most interesting and important of cellular enzymes, ATP synthase.
ATP synthase is important since it is central to the cell's production of ATP which powers a large proportion of cellular metabolism.
The ATP synthase is:
The ring rotation in turn rotates an non-symmetrical axle the in turn bonks a ring of non-rotating ATPase enzymes, changing their conformation as it goes around and catalyzing ADP plus Pi to form ATP.
It can also be driven in reverse (pumping protons) by high ATP concentrations.
This stuff was not yet taught when I took biochemistry. I only found out about ATP synthase structure and function recently. Its complexity and early evolutionary origin are remarkable.
Here is a link to a recent high resolution analysis of ATP synthase (probably pay-walled).
Among other things, he did important work on one of the most interesting and important of cellular enzymes, ATP synthase.
ATP synthase is important since it is central to the cell's production of ATP which powers a large proportion of cellular metabolism.
The ATP synthase is:
- conserved among all cellular life (indicating it was inherited from the Last Universal Common Ancestor and arose very early in life)
- large and has an extremely complex structure
- and runs on differences in proton (H+) concentrations across the cellular (or mitochondrial) membrane.
The ring rotation in turn rotates an non-symmetrical axle the in turn bonks a ring of non-rotating ATPase enzymes, changing their conformation as it goes around and catalyzing ADP plus Pi to form ATP.
It can also be driven in reverse (pumping protons) by high ATP concentrations.
This stuff was not yet taught when I took biochemistry. I only found out about ATP synthase structure and function recently. Its complexity and early evolutionary origin are remarkable.
Here is a link to a recent high resolution analysis of ATP synthase (probably pay-walled).