Enzymes
UniProtKB help_outline | 56 proteins |
Reaction participants Show >> << Hide
- Name help_outline peroxynitrite Identifier CHEBI:25941 (CAS: 19059-14-4) help_outline Charge -1 Formula NO3 InChIKeyhelp_outline CMFNMSMUKZHDEY-UHFFFAOYSA-M SMILEShelp_outline [O-]ON=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline nitrate Identifier CHEBI:17632 (Beilstein: 3587575; CAS: 14797-55-8) help_outline Charge -1 Formula NO3 InChIKeyhelp_outline NHNBFGGVMKEFGY-UHFFFAOYSA-N SMILEShelp_outline [O-][N+]([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 26 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:63116 | RHEA:63117 | RHEA:63118 | RHEA:63119 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
|||
Gene Ontology help_outline | ||||
MetaCyc help_outline |
Publications
-
Human nitrobindin: the first example of an all-beta-barrel ferric heme-protein that catalyzes peroxynitrite detoxification.
De Simone G., di Masi A., Polticelli F., Ascenzi P.
Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to <i>Homo sapiens</i>, display an all-β-barrel structural organization. Human Nb has been described as a domain of the nuclear protein named THAP4, whose physiological function is still unknown. We report the first evid ... >> More
Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to <i>Homo sapiens</i>, display an all-β-barrel structural organization. Human Nb has been described as a domain of the nuclear protein named THAP4, whose physiological function is still unknown. We report the first evidence of the heme-Fe(III)-based detoxification of peroxynitrite by the all-β-barrel <i>C</i>-terminal Nb-like domain of THAP4. Ferric human Nb (Nb(III)) catalyzes the conversion of peroxynitrite to NO 3 - and impairs the nitration of free l-tyrosine. The rate of human Nb(III)-mediated scavenging of peroxynitrite is similar to those of all-α-helical horse heart and sperm whale myoglobin and human hemoglobin, generally taken as the prototypes of all-α-helical heme-proteins. The heme-Fe(III) reactivity of all-β-barrel human Nb(III) and all-α-helical prototypical heme-proteins possibly reflects the out-to-in-plane transition of the heme-Fe(III)-atom preceding peroxynitrite binding. Human Nb(III) not only catalyzes the detoxification of peroxynitrite but also binds NO, possibly representing a target of reactive nitrogen species. << Less