Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-β-barrel structural organization. Proteins containing this domain are putatively related to fatty acid-binding proteins (FABPs) [].This domain can be found in THAP4 from mammals and At1g79260 from Arabidopsis. THAP4 catalyzes the heme-based conversion of peroxynitrite into nitrate/NO3- in vitro []. At1g79260 is a nitrophorin-like heme-binding protein that may reversibly bind nitric oxide (NO) and be involved in NO transport []. This entry also includes the β-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology [].
Nitrobindins (Nbs) are evolutionary conserved all-β-barrel heme-proteins displaying a highly solvent-exposed heme-Fe(III) atom. Mycobacterium tuberculosis Nb (Mt-Nb(III) and the C terminus of Homo sapiens Nb (Hs-Nb(III)) share this β-barrel structure, suggesting that Nb may act as a sensor possibly modulating the THAP4 transcriptional activity residing in the N-terminal region []. Ferric nitrobindin-like proteins that lack the conserved His residue which binds heme iron are also included in the Nb family.Mt-Nb(III) is a peroxynitrite isomerase that converts peroxynitrite to nitrate. It may be required to scavenge reactive nitrogen and oxygen species produced by the host during the immunity response []. In humans THAP4 catalyses the heme-based conversion of peroxynitrite into nitrate/NO3 in vitro []. At1g79260 is a nitrophorin-like heme-binding protein that may reversibly bind nitric oxide (NO) and be involved in NO transport []. This entry also includes Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology [].
This entry includes the Nitrobindin family members mostly from bacteria and plants. Mycobacterium tuberculosis Nb (Mt-Nb(III) is a peroxynitrite isomerase, which is a heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate []. This entry also includes ferric nitrobindin-like protein, lacks the conserved His residue that binds heme iron.Nitrobindins (Nbs) are evolutionary conserved all-β-barrel heme-proteins displaying a highly solvent-exposed heme-Fe(III) atom. Mycobacterium tuberculosis Nb (Mt-Nb(III) and the C terminus of Homo sapiens Nb (Hs-Nb(III)) share this β-barrel structure, suggesting that Nb may act as a sensor possibly modulating the THAP4 transcriptional activity residing in the N-terminal region []. Ferric nitrobindin-like proteins that lack the conserved His residue which binds heme iron are also included in the Nb family.
