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 …

Mesoporous materials as support for immobilized enzymes have been explored extensively
during the last two decades, primarily not only for biocatalysis applications, but also for …

Anaerobic methanotrophic archaea (ANME) carry out anaerobic oxidation of methane, thus
playing a crucial role in the methane cycle. Previous genomic evidence indicates that multi …

Proteins perform vital functional and structural duties in living systems, and the in-depth
investigation of protein in its native state is one of the most important challenges in the …

Electron transport within living cells is essential for energy conservation in all respiring and
photosynthetic organisms. While a few bacteria transport electrons over micrometer …

The heme protein cytochrome c acts as an electron carrier at the mitochondrial-membrane
interface and thus exerts its function under the influence of strong electric fields. To assess …

Cytochrome c (cyt c) is a cationic hemoprotein of∼ 100 amino acid residues that exhibits
exceptional functional versatility. While its primary function is electron transfer in the …

The mechanistic understanding of protein functions requires insight into the structural and
reaction dynamics. To elucidate these processes, a variety of experimental approaches are …

The conformational changes of bovine heart cytochrome c (cyt c) induced by the adsorption
on gold nanoparticles with different sizes have been investigated by electronic absorption …

Corrosion of iron infrastructure in anoxic environments is commonly ascribed to the
metabolic activity of sulfate-reducing bacteria (SRB), which can influence electrochemical …