Ferredoxins are a group of iron–sulfur proteins for which a wealth of structural and
mutational data have recently become available. Previously unknown structures of …

Nocardioides sp. strain KP7 grows on phenanthrene but not on naphthalene. This organism
degrades phenanthrene via 1-hydroxy-2-naphthoate, o-phthalate, and protocatechuate. The …

The use of a short, three-residue Cu2+-binding sequence, the ATCUN motif, is presented as
an approach for extracting long-range distance restraints from relaxation enhancement NMR …

At the beginning of the 1990s, when obtaining solution structures of biomolecules by nuclear
magnetic resonance (NMR) was already a well-established technique, it was commonly …

The solution structure of the dicerium (III) complex of the N-terminal domain of calmodulin
(Ce2-TR1C hereafter) has been solved employing paramagnetic T 1 relaxation …

The proteins responsible for controlling electron transfer in bacterial secondary metabolism
are not always known or characterised. Here we demonstrate that many bacteria contain a …

Members of the fusion-associated small transmembrane (FAST) protein family are a distinct
class of membrane fusion proteins encoded by nonenveloped fusogenic reoviruses. The …

A [2Fe-2S] ferredoxin (Fd1) from the hyperthermophilic bacterium Aquifex aeolicus has been
obtained by heterologous expression of the encoding gene in Escherichia coli. Sequence …

The orientation and the axial, Δχax, and rhombic, Δχrh, components of the magnetic
susceptibility tensor anisotropy for the cobalt (II) and nickel (II) derivatives of azurin from …

Ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus is a monomeric
protein (7.5 kDa) that contains a single [4Fe-4S] 1+, 2+ cluster. The protein is unusual in that …