The “Watchmaker” argument asserts that as the intricacy of a watch implies the mind and work of a watchmaker, so the complexity of an organism also implies the work of an Intelligent Designer. Skeptics, in attacking the Watchmaker argument, challenge the necessity of a Creator’s existence from the study of nature, saying that at best, only a weak analogy exists between a watch and nature. However, recent discoveries showing detailed similarities between biomolecular motors and man-made machines revitalize and add a powerful dynamic to the Watchmaker argument for an Intelligent Designer.1
Biomolecular motors generate movement within a cell. Several of these protein/enzyme ensembles, as well as other enzymes, possess components functioning as strict analogs to man-made machine parts.2 The remarkable resemblance of these biomolecular motors’ (machines by definition) to man-made machines may hold the key to unlocking future technological advance.
The inability to power motion in nanodevices (molecular-sized constructs made by engineering molecules and organized into a precise arrangement) stands as one of the major barriers preventing nanotechnology from becoming viable. The Sixth Foresight Conference on Molecular Nanotechnology (held in November 1998) revealed an important first step towards achieving powered motion in nanodevices. Scientists from Cornell and an independent group from the University of Washington in Seattle reported the feasibility of using biomolecular motors to power man-made molecular devices.3
Advancing earlier feasibility studies, Cornell University scientists produced a hybrid nanomechanical device powered by a biomolecular motor.4 With dimensions of less than 1,000 nanometers (1 billion nanometers equals 1 meter), nanodevices possess potential applications in manufacturing, electronics, and medicine. Using biomolecular motors to power man-made nanodevices “drives home” the machine-like character of biomolecular motors.
The particular biomolecular motor employed by the Cornell scientists, F1-F0 ATPase, plays a central role in harvesting energy for cellular use.5 F1-F0 ATPase is a mushroom-shaped enzyme complex that possesses a turbine, rotor, and stator.
The Cornell researchers attached nickel nanopropellers to the F1-F0 ATPase rotor. Upon the addition of ATP—a chemical compound that powers the F1-F0 ATPase rotor—the nanopropellers rotated at a velocity of 0.74 to 8.3 revolutions per second. The F1-F0 ATPase-powered nanodevice operated at nearly 80 percent efficiency (compared with the 20 percent efficiency of an automobile engine).
The structures of biomolecular assemblies not only highlight the similarity between cellular and man-made machines, but also reflect the knowledge and intelligence of the one who engineered them. Biomolecular machines display far more complex, efficient, and elegant design than anything humans can engineer.
Research in nanotechnology continues to expose the difficulty of mimicking in the laboratory that which nature does readily. Working at a molecular level, scientists have been unable, in any practical sense, to build a synthetic molecular motor capable of powering nanodevices. In the words of one researcher actively investigating F1-F0 ATPase, “We couldn’t ever build a motor that small—but nature has.”6 In light of this comparison, does it really make sense to view these tiny, complex, and efficient biological molecular motors as the simple product of blind, random biochemical events?
- Fazale Rana and Micah Lott, “Hume vs. Paley: These ‘Motors’ Settle the Debate,” Facts for Faith 2, (Q2 2000), 34-39.
- Rana and Lott, 34-39.
- Robert F. Service, “Borrowing from Biology to Power the Petite,” Science 283 (1999), 27-28.
- Ricky K. Soong et al., “Powering an Inorganic Nanodevice with a Biomolecular Motor,” Science 290 (2000), 1555-58.
- Matti Saraste, “Oxidative Phospherylation at the Fin de Siècle,” Science 283 (1999), 1488-93.
- Helen Pearson, “Japanese Take Revolutionary Snapshots,” Nature Science Updates, April 19, 2001. Available from http://www.nature.com/nsu/010419/010419-3.html; accessed October 24, 2001.