Albumin nitrosylated

Reactions of NO were also studied with the synthetic heme protein discussed earlier, namely the recombinant human serum albumin (rHSA) with eight incorporated TPPFe derivatives bearing a covalently linked axial base, were also investigated. The UV-vis absorption spectrum of the phosphate buffer solution at physiological pH showed absorption band maxima at 425 and 546 nm upon the addition of NO to form the nitrosyl species, which was also formed when the six-coordinate CO-adducts were reacted with NO gas. EPR spectroscopy revealed that the albumin-incorporated iron(II) porphyrin formed six-coordinate nitrosyl complexes. It was observed that the proximal imidazole moiety does not dissociate from the central iron when NO binds to the trans position. The NO-binding affinity P1 /2no was 1.7 X 10 torr at pH 7.3 and 298 K, significantly lower than that of the porphyrin complex itself, and was interpreted as arising from the decreased association rate constant (kon(NO), 8.9 x 10 M s" -1.5 x 10 M s ). Since NO-association is diffusion controlled, incorporation of the synthetic heme into the albumin matrix appears to restrict NO access to the central iron(II). ... 

Nitrosylated albumin was detected in activated macrophage supernatants using an anti-NO-acetyl-ated cysteine antibody (Gobert et al. 1999). It was estimated that 10 % of N2O3 produced by activated cells participate in extracellular nitrosylation. N2O3 thus appears to be a new effector molecule of the immune system, as an agent for the nitrosylation of albumin, the main nitric oxide carrier in vivo. 

Ishima, Y, Akaike, T, Kragh-Hansen, U., Hiroyama, S., Sawa, T, Suenaga, A., Maruyama, T., Kai, T., and Otagiri, M. (2008). S-Nitrosylated human serum albumin-mediated cytoprotective activity is enhanced by fatty acid binding. J. Biol. Chem. 283, 34966-34975. 

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