Ferredoxins are a group of iron-sulfur proteins for which a wealth of
structural and mutational data have recently become available. Previou
sly unknown structures of ferredoxins which are adapted to halophilic,
acidophilic or hyperthermophilic environments and new cysteine patter
ns for cluster ligation and non-cysteine cluster ligation have been de
scribed. Site-directed mutagenesis experiments have given insight into
factors that influence the geometry, stability, redox potential, elec
tronic properties and electron-transfer reactivity of iron-sulfur clus
ters. (C) 1998 Elsevier Science Ltd. All rights reserved.