Cytochrome c', a c-type cytochrome with unique spectroscopic and magnetic properties, has been characterized in a variety of denitrifying and photosynthetic bacteria. Cytochrome c' has a role in defence and/or removal of NO but the mechanism of action is not clear. To examine the function of cytochrome c' from Neisseria meningitidis, the protein was purified after heterologous overexpression in...

In the title mol-ecule, [Fe(2)(C(5)H(5))(2)(C(17)H(16)Si)], the cyclo-penta-dienyl rings linked to the same Fe atom are approximately eclipsed and the inter-planar angles are 1.8 (2) and 3.4 (2)°. The Fe atom is slightly closer to the substituted cyclo-penta-dienyl ring.

The redox-active metallaphosphine [Fe(dppe)(η(5)-C5Me5)(C≡C-PPh2)] reacts with [Pd(1,5-cod)Cl2] to give mono- and bis-phosphine coordinated palladium centres as a function of stoichiometry, and these complexes provide a stable redox-active platform which allows reversible one-electron {Fe(II)→Fe(III)(+)} oxidations within the palladium coordination sphere.

In the title compound, [Fe(2)(C(7)H(4)IN)(C(3)H(6)S(2))(CO)(5)], the Fe-Fe distance of 2.5156 (11) Å compares well with that in related model structures. The phenyl isocyanide ligand is in the basal position and trans to the S atoms of the propane-dithiol-ate ligand due to steric hindrance. The crystal structure features C-H⋯O inter-actions.

Measurements with the selected-ion flow tube technique are reported for the room-temperature kinetics of the sequential ligation of Fe and (c-C5H5)Fe with HCN and HC3N in helium bath gas at 0.35 Torr. (c-C5H5)2Fe was observed not to react. Titration curves of the variation in the apparent bimolecular rate coefficient for ligation with the number of ligands provide cyanide coordination numbers f...

Reduced (Fe(II)) Rhodopseudomonas palustris cytochrome c' (Cyt c') is more stable toward unfolding ([GuHCl](1/2) = 2.9(1) M) than the oxidized (Fe(III)) protein ([GuHCl](1/2) = 1.9(1) M). The difference in folding free energies (Delta Delta G(f) degrees = 70 meV) is less than half of the difference in reduction potentials of the folded protein (100 mV vs. NHE) and a free heme in aqueous solutio...