Background: SaFtsZ crystallizes in the form of assembled straight protofilaments, with large scale sliding/rotation of its subdomains relative to monomeric FtsZ. Results: Mutants of the T7 loop also crystallized as protofilaments, but the subdomain movement was quite variable. Conclusion: Subdomain movement is strongly correlated with intermolecular interactions via the T7 loop. Significance: Subdomain movement generates GTPase active protofilament and induces the straight to curved conformational change.

In our previous paper, we synthesized poly-3-hydroxybutyrate [P(3HB)] by using the waterorganic-solvent two-phase reaction system (TPRS), in which (R)-3-hydroxybutyrylCoA [(R)-3HBCoA] was continuously supplied to PHA synthase by the ester exchange reaction between CoA and thiophenol in thiophenyl (R)-3HB [(R)-3HBTP]. By applying TPRS to the screening, we found a lactate-(LA-) polymerizing enzyme from PHA synthases. The enzyme was an engineered PHA synthase, which stereoselectively copolymerized (R)-LA together with (R)-3HB. NMR and GPC revealed that the TPRS successfully synthesized poly(lactate-co-(3-hydroxybutyrate)) [P(LA-co-3HB)] using the LA-polymerizing enzyme as a catalyst. The molar ratios of LA in the copolymers were controllable in the range of 0 to 36 mol% by varying the ratio of (R)-LATP and (R)-3HBTP fed into the TPRS. The number-average molecular weight and the polydispersity of P(36 mol%-co-3HB) were 1.1 × 10 4 and 1.4, respectively. This is the first report on the chemo-enzymatic synthesis of P(LA-co-3HB) by a LA-polymerizing enzyme.

A 3D Pt/TiO2 architecture assembled from 1D nanowires has been designed and successfully prepared by an environmentally-friendly one-pot solvothermal process. The formation mechanism has been investigated and the unique architecture exhibits an excellent photocatalytic hydrogen production rate as high as 13.33 mmol h(-1) g(-1), the corresponding apparent quantum efficiency reaches 34%.

A previously established improved two-phase reaction system has been applied to analyze the substrate specificities and polymerization activities of polyhydroxyalkanoate (PHA) synthases. We first analyzed the substrate specificity of propionate coenzyme A (CoA) transferase and found that 2-hydroxybutyrate (2HB) was converted into its CoA derivative. Then, the synthesis of PHA incorporating 2HB was achieved by a wild-type class I PHA synthase from Ralstonia eutropha. The PHA synthase stereoselectively polymerized (R)-2HB, and the maximal molar ratio of 2HB in the polymer was 9 mol%. The yields and the molecular weights of the products were decreased with the increase of the (R)-2HB concentration in the reaction mixture. The weight-average molecular weight of the polymer incorporating 9 mol% 2HB was 1.00 × 10(5), and a unimodal peak with polydispersity of 3.1 was observed in the GPC chart. Thermal properties of the polymer incorporating 9 mol% 2HB were analyzed by DSC and TG-DTA. T (g), T (m), and T (d) (10%) were observed at -1.1°C, 158.8°C, and 252.7°C, respectively. In general, major components of PHAs are 3-hydroxyalkanoates, and only engineered class II PHA synthases have been reported as enzymes having the ability to polymerize HA with the hydroxyl group at C2 position. Thus, this is the first report to demonstrate that wild-type class I PHA synthase was able to polymerize 2HB.

No abstract