Biological inorganic chemistry at the beginning of the 21st century

Abstract

Advances in bioinorganic chemistry since the 1970s have been driven by three factors: rapid determination of high-resolution structures of proteins and other biomolecules, utilization of powerful spectroscopic tools for studies of both structures and dynamics, and the widespread use of macromolecular engineering to create new biologically relevant structures. Today, very large molecules can be manipulated at will, with the result that certain proteins and nucleic acids themselves have become versatile model systems for elucidating biological function.

Figure 1

View of membrane-bound cytochrome c oxidase showing two of the proposed proton-pumping pathways as well as the site where dioxygen is reduced to water (adapted from ref. 14).

Figure 2

Structure of the nitrogenase active site core showing the location of a nitrogen (or possibly a carbon or oxygen) atom (blue) embedded in a cluster of seven iron atoms (gray), one molybdenum (cyan), and nine bridging sulfurs (yellow) (adapted from ref. 87).

Figure 3

Cytochrome c folding energy landscapes: (Upper) profiles illustrating different ligand substitution barriers for the Co, Fe, and Zn proteins; (Lower) idealized three-dimensional representation of the landscape for the native protein (adapted from refs. and 162).