Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …

The synthetic analogue approach to the metal sites in iron-sulfur proteins was initiated in the
early 1970s. Structures of sites 1-8 defined by X-ray crystallography are collected in Figure …

An account is given of the development of the SHELX system of computer programs from
SHELX-76 to the present day. In addition to identifying useful innovations that have come …

The ligand K-edge probes the ligand 1s→ valence np transitions. These transitions acquire
intensity when the ligand is bound to an open shell metal ion. This intensity quantifies the …

The geometry of metal–ligand interactions in proteins is examined and compared with
information for small-molecule complexes from the Cambridge Structural Database (CSD) …

Recent advances in ab initio direct methods have enabled the solution of crystal structures
of small proteins from native X-ray data alone, that is, without the use of fragments of known …

A set of tables is presented and a survey given of the architecture of metal coordination
groups in a representative set of protein structures from the Protein Data Bank [Bernstein et …

Complex iron-sulfur metalloclusters form the active sites of the enzymes that catalyze redox
transformations of N2, CO, and H2, which are likely components of Earth's primordial …

Metals are present in more than one-third of all proteins as they occur in nature, and are
usually important in biological function or maintenance of the structure. Some are present as …

The reaction center (RC) of photosynthetic bacteria is a membrane protein complex that
promotes a light-induced charge separation during the primary process of photosynthesis. In …