Nitric oxide (NO) is an inevitable product of life in an oxygen-and nitrogen-rich environment.
This reactive diatomic molecule exhibits microbial cytotoxicity, in large part by facilitating …

The iron (II)–dioxygen bond in myoglobin and hemoglobin is a subject of wide interest.
Studies range from examinations of physical–chemical properties dependent on its …

NADPH is a system in phagocytic cells that generates O2− and hydrogen peroxide in the
endocytic vacuole, both of which are important for killing of the engulfed microbe …

The process of oxygen-dependent hemoglobin induction in Daphnia magna was studied
over an 11-day period of hypoxia (ambient oxygen partial pressure: 3 kPa). Along with the …

Globin‐like oxygen‐binding proteins occur in bacteria, yeasts and other fungi, and protozoa.
The simplest contain protohaem as sole prosthetic group, but show considerable variation in …

Lucina pectinata live in high concentrations of hydrogen sulfide (H 2 S) and contains one
hemoglobin, Hemoglobin I (HbI), transporting H 2 S and two hemoglobins, Hemoglobin II …

Escherichia coli flavohaemoglobin (Hmp) reduced purified mitochondrial cytochrome c
aerobically in a reaction that was not substantially inhibited by superoxide dismutase …

Small size globins that have been defined as 'truncated haemoglobins' or as '2/2
haemoglobins' have increasingly been discovered in microorganisms since the early 1990s …

Escherichia coli flavohemoglobin (HMP) is shown to be capable of catalyzing the reduction
of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as …