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

Covering: up to 2006The heme prosthetic group is vital to many cellular processes and is
therefore widespread throughout organisms of different phylogenetic origin. Heme is used in …

The effect of axial ligand nodal plane orientation on the contact and pseudocontact shifts of
a symmetrical low-spin octamethylferriheme center has been calculated as a function of the …

The family of b 5-like cytochromes encompasses, besides cytochrome b 5 itself,
hemoprotein domains covalently associated with other redox proteins, in flavocytochrome b …

The different paramagnetic shifts of the four methyl groups in ferriheme proteins have been
described as being due to the effect of the axial ligand nodal plane orientation. An equation …

Heme binds selectively to the 3′-terminal G-quartet of all parallel G-quadruplex DNAs to
form stable heme–DNA complexes. Interestingly, the heme–DNA complexes exhibit various …

The heme group in paramagnetic (S= 1/2) ferricytochromes c typically displays a markedly
asymmetric distribution of unpaired electron spin density among the heme pyrrole β …

The solution structure of oxidized rat microsomal cytochrome b 5 has been obtained from 1H
NMR spectra measured at 800 MHz. The available assignment has been extended to 78 …

Isotope effects on chemical shifts, nΔ 13C (D), nΔ 1H (D), 1Δ 15N (D) and 1Δ 13C (18O),
and solvent isotope effects in proteins are reviewed and references are provided to related …

Despite the wealth of information that has been obtained from the study of paramagnetic
hemes and heme proteins by 1 H NMR spectroscopy, there are certain limitations imposed …