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 …

Significance: Acrylamide (AA) widely exists in the environment. Studies have demonstrated
that AA has neurotoxicity and potential carcinogenicity in humans, and genotoxicity and …

Nitrogen-vacancy (NV) magnetometry offers an alternative tool to detect paramagnetic
centers in cells with a favorable combination of magnetic sensitivity and spatial resolution …

Cable bacteria embed a network of conductive protein fibers in their cell envelope that
efficiently guides electron transport over distances spanning up to several centimeters. This …

Two models have been proposed to explain the interaction of cytochrome c with cardiolipin
(CL) vesicles. In one case, an acyl chain of the phospholipid accommodates into a …

Cytochrome c undergoes structural variations during the apoptotic process; such changes
have been related to modifications occurring in the protein when it forms a complex with …

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 …

We report a resonance Raman and UV–vis characterization of the active site structure of
oxidatively modified forms of cytochrome c (Cyt-c) free in solution and in complexes with …

Hemoproteins include several heme-binding proteins with distinct structure and function.
The presence of the heme group confers specific reactivity and spectroscopic properties to …

Phosphorylation of tyrosine 48 of cytochrome c is related to a wide range of human diseases
due to the pleiotropic role of the heme‐protein in cell life and death. However, the structural …