We will also look to the chemical details of biology for lessons in how to carry out complex and important reactions under mild conditions. Today, the chemical industry produces ammonia from nitrogen through a high-temperature, high-pressure reaction that consumes lots of energy, yet microorganisms are capable of carrying out the same reaction at normal pressures and temperatures within the environment of the cell, using a metalloprotein catalyst called nitrogenase. Structural insights into this and other remarkable metalloprotein catalysts have recently become available. But can we now harness that understanding to develop new methods and new small molecular catalysts that incorporate the key attributes of the natural enzymes? Many of these enzymes, nitrogenase in particular, are capable of activating small, abundant, basically inert molecules through multielectron reactions. A tremendous challenge to the chemist lies in the design and application of catalysts, whether small molecules or materials, that can carry out such multielectron transfers to activate small molecules such as nitrogen, oxygen, and methane. Imitating some aspects of life, biomimetic chemistry is not the only way to invent new things, but it is one of the ways.

We will look to chemical biology for guidance not only in designing new smaller catalysts but also in devising methods to assemble large molecular machines. Replication, transcription, and translation, as well as other critical cellular functions, appear to be carried out through the function of multiprotein/nucleic acid particles. Advances in x-ray crystallography coupled with other imaging methods such as NMR and electron microscopy are now providing our first snapshots of these macromolecular machines, such as the ribosome in which proteins are synthesized in the cell. A spectacular recent advance is the determination of