The modification of protein cysteine residues underlies some of the diverse biological
functions of nitric oxide (NO) in physiology and disease. The formation of stable nitrosothiols …

Abstract l-Tryptophan is an essential amino acid for mammals. It is utilized not only for
protein synthesis but also for the biosynthesis of serotonin and melatonin by the serotonin …

Dinitrosyl iron complexes (DNICs) are a physiological form of nitric oxide (• NO) in an
organism. They are able not only to deposit and transport• NO, but are also to act as …

The heme enzyme indoleamine 2, 3-dioxygenase (IDO) is a key regulator of immune
responses through catalyzing l-tryptophan (l-Trp) oxidation. Here, we show that hydrogen …

Cellular damage occurring under oxidative conditions has been ascribed mainly to the
formation of peroxynitrite (ONOOH/ONOO−) that originates from the reaction of NO• with …

The nuclear genome of the model organism Chlamydomonas reinhardtii contains genes for
a dozen hemoglobins of the truncated lineage. Of those, THB1 is known to be expressed …

Rapid secretion of eosinophil-associated RNases (EARs), such as the human eosinophilic
cationic protein (ECP), from intracellular granules is central to the role of eosinophils in …

Cyanobacterium Synechococcus sp. PCC 7002 contains a single gene (glbN) coding for
GlbN, a protein of the 2/2 hemoglobin lineage. The precise function of GlbN is not known …

During catalysis, the heme in nitric oxide synthase (NOS) binds NO before releasing it to the
environment. Oxidation of the NOS ferrous heme–NO complex by O2 is key for catalytic …

Hemoglobin and myoglobin are generally taken as molecular models of all-α-helical heme-
proteins. On the other hand, nitrophorins and nitrobindins (Nb), which are arranged in 8 and …