High impact information on Mesobiliverdin

• The structures of ternary complexes with mesobiliverdin IValpha, biliverdin IXalpha, FMN and lumichrome show that human BVR-B has a single substrate binding site, to which substrates and inhibitors bind primarily through hydrophobic interactions, explaining its broad specificity [1].
• Fast atom bombardment mass spectroscopy shows the masses of the alpha-1 MBV and beta-1 MBV peptides to be 2 atomic mass units lower than those of the alpha-1 PCB and beta-1 PCB peptides, respectively [2].
• Contrary to what is observed with biliverdin-IX alpha, 4, the enzymatic reduction of the mesobiliverdin derivative 2-MPEGA to the corresponding mesobilirubin 3-MPEGA by the soluble biliverdin reductase/NADPH system in pH 7.4 aqueous phosphate does not occur [3].
• The complex was fairly stable in air, but when the complex was incubated with the NADPH-cytochrome c reductase system, the hydroxymesoheme bound to heme oxygenase was readily converted to mesobiliverdin through the 660 nm compound as an intermediate [4].

Associations of Mesobiliverdin with other chemical compounds

• Mesoheme bound to heme oxygenase protein was easily degraded to mesobiliverdin by incubation with NADPH-cytochrome c reductase and NADPH [4].

Analytical, diagnostic and therapeutic context of Mesobiliverdin

• With mesoheme as the substrate, the reaction product was identified as mesobiliverdin IX alpha by spectrophotometry and reverse-phase HPLC [5].
• Mesobiliverdin IX alpha was identified as the primary incubation product by comparative reverse-phase high-pressure liquid chromatography and absorption spectrophotometry [6].

References