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 …

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 …

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 …

Conspectus Hemes are ubiquitous in biology and carry out a wide range of functions. The
heme group is largely invariant across proteins with different functions, although there are a …

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 …

Out-of-plane (OOP) deformations of the heme cofactor are found in numerous heme-
containing proteins and the type of deformation tends to be conserved within functionally …

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 …

Protein structures respond to changes in their chemical and physical environment. However,
studying such conformational changes is notoriously difficult, as many structural biology …

We describe a simple method for the determination of heme protein reduction potentials. We
use the method to determine the reduction potentials for the PAS-A domains of the …

Heme proteins are known to perform a plethora of biologically important functions. This
article reviews work that has been conducted on various class I cytochrome c proteins over a …