Publisher Summary A growing number of homo-and heterodimeric hemoglobins have been
identified not only within several phyla of invertebrates and lower vertebrates, but also in …

Many pathogenic microorganisms have evolved hemoglobin-mediated nitric oxide (NO)
detoxification mechanisms, where a globin domain in conjunction with a partner reductase …

The modification of myoglobin is an attractive process not only for understanding its
molecular mechanism but also for engineering the protein function. The strategy of …

The hemoglobin from the marine worm Amphitrite ornata has been found to possess
multiple enzymatic activities in addition to its O 2-transport function. Named …

The proximal side of dehaloperoxidase-hemoglobin A (DHP A) from Amphitrite ornata has
been modified via site-directed mutagenesis of methionine 86 into aspartate (M86D) to …

There are many examples of oxidative enzymes containing both flavin and heme prosthetic
groups that carry out the oxidation of their substrate. For the purpose of this article we have …

Due to their functional independence, proteins that comprise standalone metabolic units,
which we name single-protein metabolic modules, may be particularly prone to gene …

The flavin dependent nonheme diiron proteins comprise a family of enzymes, which can act
as scavengers for both molecular oxygen and nitric oxide. The reduction of nitric oxide to …

Flavin‐dependent monooxygenases (FMOs) constitute a diverse enzyme family that
catalyzes crucial hydroxylation, epoxidation, and Baeyer–Villiger reactions across various …

Bacterial hemoglobins play important roles inside the cell. Phylogenetically, they belong to
three different families: the single domain hemoglobin, flavohemoglobin and truncated …