Nitric oxide transport protein

Hoshino M, Maeda M, Konishi R, Seki H, Ford PC. Studies on the reaction mechanism for reductive nitrosylation of ferrihemopro-teins in buffer solutions. J. Am. Chem. Soc. 1996 118 5702-5707. Weichsel A, Maes EM, Andersen JF, Valenzuela JG, Shokhireva T, Walker FA, Montfort WR. Heme-assisted S-nitrosation of a proximal thiolate in a nitric oxide transport protein. Proc. Natl. Acad. Sci. U. S. A. 2005 102 594-599. 

A. Weichsel, J.F. Andersen, D.E. Champagne, F.A. Walker and W.R. Montfort (1998) Nature Structural Biology, vol. 5, p. 304 - Crystal structures of a nitric oxide transport protein from a blood-sucking insect . 

Due to its versatile role, nitric oxide transport within proteins is particularly intensively studied (Marti et al. 2008). 

Proteins associated with the PDZ ligand of the 5-HT4e receptor C-terminus are completely different from those that bind to the 5-HT4a receptors. They include the neuronal isoform of nitric oxide synthase (nNOS) and CIPP, two PDZ-domain-containing proteins, and Sec 23, which lacks any obvious PDZ domain (9). Sec 23 is a member of a protein complex designated as COPII, which is involved in the budding of vesicles from the endoplasmic reticulum (ER) and ER-to-Golgi transport of proteins. 

Cytochrome cdj needs three things to reduee nitrite to nitric oxide, substrates nitrite and protons plus eleetrons. The first two are simply supplied from the environment but where do the eleetrons eome from Cytochrome cdi derives its electrons from the eleetron transport system in the cytoplasmic membranes of baeteria. Thus, for example, eleetrons ean originate from NADH and pass via NADH dehydrogenase, ubiquinone/ubiquinol and the cytochrome bc eomplex to nitrite reduetase (Berks et al., 1995 Zumft, 1997). It is known that the eytoehrome bc eomplex is used beeause electron transfer from physiologieal donors, e.g. NADH, to nitrite reduetase is blocked by specific inhibitors, e.g. myxothiazol, of this complex. An important issue arises when we eonsider how electrons are transferred from the cytochrome fccj complex to eytoehrome cd, which, recall, is a water-soluble protein located in the periplasm. The structure of the cytochrome be I complex (determined for the mitoehondrial protein but we can assume that the bacterial counterparts are similarly organised) shows that the... 

Moir, J. W. B., and Ferguson, S. J., 1994, Properties of a Paracoccus denitrificans mutant deleted in cytochrome C550 indicate that a copper protein can substitute for this cytochrome in electron transport to nitrite, nitric oxide and nitrous oxide. Microbiology 140 3989397. 

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