Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible
structure, particularly in the ferric form, such that it is able to sample a broad conformational …

Paramagnetic centers in biomolecules, such as specific metal ions that are bound to a
protein, affect the nuclei in their surrounding in various ways. One of these effects is the …

This article deals with the solution structure determination of paramagnetic metalloproteins
by NMR spectroscopy. These proteins were believed not to be suitable for NMR …

Covering: up to July 2008 A discussion of the literature concerning the synthesis, function,
and activity of hemec-containing proteins is presented. Comparison of the properties of …

At the onset of apoptosis, the peroxidation of cardiolipin at the inner mitochondrial
membrane by cytochrome c requires an open coordination site on the heme. We report a …

Cytochrome c, a mitochondrial electron transfer protein containing a hexacoordinated heme,
is involved in other physiologically relevant events, such as the triggering of apoptosis, and …

Six‐coordinated heme groups are involved in a large variety of electron transfer reactions
because of their ability to exist in both the ferrous (Fe2+) and ferric (Fe3+) state without any …

Spectrally resolved stimulated vibrational echo spectroscopy is used to investigate the
dependence of fast protein dynamics on bulk solution viscosity at room temperature in four …

Examining electron transfer between two proteins with identical spectroscopic signatures is
a challenging task. It is supposed that several multiheme cytochromes in Shewanella …

We report here the chemical bonding and aromaticity patterns in metalloporphyrins, which
were obtained with density functional theory (DFT) calculations at the OPBE/TZP level. This …