Light-driven chemical transformations provide a compelling approach to understanding
chemical reactivity with the potential to use this understanding to advance solar energy and …

Light-induced microbial electron transfer has potential for efficient production of value-added
chemicals, biofuels and biodegradable materials owing to diversified metabolic pathways …

The multifunctional protein cytochrome c (cyt c) plays key roles in electron transport and
apoptosis, switching function by modulating bonding between a heme iron and the sulfur in …

Physiological bond formation and bond breaking events between proteins and ligands and
their immediate consequences are difficult to synchronize and study in general. However …

Computational modeling can provide a wealth of insight into how energy flow in proteins
mediates protein function. Computational methods can also address fundamental questions …

Cytochrome (cyt) c is an important electron transfer protein. The ruffling deformation of its
heme cofactor has been suggested to relate to its electron transfer rate. However, there is no …

The structure–function relationship is at the heart of biology, and major protein deformations
are correlated to specific functions. For ferrous heme proteins, doming is associated with the …

In haemoglobin the change from the low-spin (LS) hexacoordinated haem to the high spin
(HS, S= 2) pentacoordinated domed deoxy-myoglobin (deoxyMb) form upon ligand …

Some classes of bacteria within phyla possess protein sensors identified as homologous to
the heme domain of soluble guanylate cyclase, the mammalian NO-receptor. Named H-NOX …

Axial Cu–S (Met) bonds in electron transfer (ET) active sites are generally found to lower
their reduction potentials. An axial S (Met) bond is also present in cytochrome c (cyt c) and is …