Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …

This review regards the use of dynamic electrochemistry to study the mechanism of redox
enzymes, with exclusive emphasis on the configuration where the protein is adsorbed onto …

This review is focused on the basic principles, the main applications, and the theoretical
models developed for various redox mechanisms in protein film voltammetry, with a special …

While iron is often a limiting nutrient to Biology, when the element is found in the form of
heme cofactors (iron protoporphyrin IX), living systems have excelled at modifying 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 …

Splitting the reduction potential of electron transport (ET) proteins and redox
metalloenzymes into the enthalpic and entropic contributions is an insightful practice to …

Cytochrome c nitrite reductases (C c NIR or NrfA) play important roles in the global nitrogen
cycle by conserving the usable nitrogen in the soil. Here, the electron storage and …

Cytochrome c 6A is a unique dithio-cytochrome of green algae and plants. It has a very
similar core structure to that of bacterial and algal cytochromes c 6 but is unable to fulfill the …

Hydrogen exchange (HX) rates and midpoint potentials (E m) of variants of cytochrome c
from Pseudomonas aeruginosa (Pa cyt c 551) and Hydrogenobacter thermophilus (Ht cyt c …

Heme c is characterized by its covalent attachment to a polypeptide. The attachment is
typically to a CXXCH motif in which the two Cys form thioether bonds with the heme,“X” can …