Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential
for O 2 transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a …

Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

The FixL proteins are biological oxygen sensors that restrict the expression of specific genes
to hypoxic conditions. FixL's oxygen-detecting domain is a heme binding region that controls …

In a great variety of organisms throughout all kingdoms of life, the heme-based-sensor
proteins are the key regulators of adaptive responses to fluctuating oxygen, carbon …

The nature of the Fe− O2 bonding in oxy-myoglobin was probed by theoretical
calculations:(a) QM/MM (hybrid quantum mechanical/molecular mechanical) calculations …

The effects of mutagenesis on geminate and bimolecular O 2 rebinding to 90 mutants at 27
different positions were used to map pathways for ligand movement into and out of sperm …

An overview of the application of Fourier transform infrared spectroscopy for the analysis of
the structure of proteins and protein–ligand recognition is given. The principle of the …

Myoglobin (Mb) is perhaps the most studied protein, experimentally and theoretically.
Despite the wealth of known details regarding the gas migration processes inside Mb, there …

Using the CASSCF/CASPT2 approach, along with several DFT methods (PBE0, B3LYP,
BP86, OLYP), we have investigated the bonding of CO, NO, and O2 molecules to two model …

A direct sensor of O2, the Dos protein, has been found in Escherichia coli. Previously, the
only biological sensors known to respond to O2 by direct and reversible binding were the …