Search results
Results From The WOW.Com Content Network
Nitric oxide reacts with transition metals to give complexes called metal nitrosyls. The most common bonding mode of nitric oxide is the terminal linear type (M−NO). [6] Alternatively, nitric oxide can serve as a one-electron pseudohalide. In such complexes, the M−N−O group is characterized by an angle between 120° and 140°.
A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. [1] They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes.
Nitric oxide (nitrogen monoxide) is a molecule and chemical compound with chemical formula of N O. In mammals including humans, nitric oxide is a signaling molecule involved in several physiological and pathological processes. [1] It is a powerful vasodilator with a half-life of a few seconds in the blood.
Nitric oxide synthases (EC 1.14.13.39) (NOSs) are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone , insulin secretion, airway tone, and peristalsis , and is involved in angiogenesis and neural development.
S-Nitrosoglutathione (GSNO) is an endogenous S -nitrosothiol (SNO) that plays a critical role in nitric oxide (NO) signaling and is a source of bioavailable NO. NO coexists in cells with SNOs that serve as endogenous NO carriers and donors. SNOs spontaneously release NO at different rates and can be powerful terminators of free radical chain ...
These complexes are isoelectronic and, incidentally, both obey the 18-electron rule. The formal description of nitric oxide as NO + does not match certain measureable and calculated properties. In an alternative description, nitric oxide serves as a 3-electron donor, and the metal-nitrogen interaction is a triple bond. linear and bent M-NO bonds
Heme (American English), or haem (Commonwealth English, both pronounced / hi:m / HEEM), is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. [1]
S. -Nitrosylation. In biochemistry, S-nitrosylation is the covalent attachment of a nitric oxide group (−NO) to a cysteine thiol within a protein to form an S -nitrosothiol (SNO). S -Nitrosylation has diverse regulatory roles in bacteria, yeast and plants and in all mammalian cells. [1] It thus operates as a fundamental mechanism for cellular ...