02815nas a2200241   4500008004100000022001400041245014600055210006900201260009000270300001800360490000600378520190300384100001502287700001402302700001402316700001502330700002202345700001802367700002002385700001702405700002502422856012602447       2005                        eng d  a1475-285900aInactive enzymatic mutant proteins (phosphoglycerate mutase and enolase) as sugar binders for ribulose-1,5-bisphosphate regeneration reactors0 aInactive enzymatic mutant proteins phosphoglycerate mutase and e  aMIDDLESEX HOUSE, 34-42 CLEVELAND ST, LONDON W1T 4LB, ENGLANDbBIOMED CENTRAL LTDcFEB  aArticle No. 50 v43 a<p>Background: Carbon dioxide fixation bioprocess in reactors necessitates recycling of D- ribulose1,5-bisphosphate (RuBP) for continuous operation. A radically new close loop of RuBP regenerating reactor design has been proposed that will harbor enzyme-complexes instead of purified enzymes. These reactors will need binders enabling selective capture and release of sugar and intermediate metabolites enabling specific conversions during regeneration. In the current manuscript we describe properties of proteins that will act as potential binders in RuBP regeneration reactors. Results: We demonstrate specific binding of 3-phosphoglycerate (3PGA) and 3-phosphoglyceraldehyde ( 3PGAL) from sugar mixtures by inactive mutant of yeast enzymes phosphoglycerate mutase and enolase. The reversibility in binding with respect to pH and EDTA has also been shown. No chemical conversion of incubated sugars or sugar intermediate metabolites were found by the inactive enzymatic proteins. The dissociation constants for sugar metabolites are in the micromolar range, both proteins showed lower dissociation constant (Kd) for 3-phosphoglycerate ( 655 - 796 mu M) compared to 3-phosphoglyceraldehyde ( 822 - 966 mu M) indicating higher affinity for 3PGA. The proteins did not show binding to glucose, sucrose or fructose within the sensitivity limits of detection. Phosphoglycerate mutase showed slightly lower stability on repeated use than enolase mutants. Conclusions: The sugar and their intermediate metabolite binders may have a useful role in RuBP regeneration reactors. The reversibility of binding with respect to changes in physicochemical factors and stability when subjected to repeated changes in these conditions are expected to make the mutant proteins candidates for in-situ removal of sugar intermediate metabolites for forward driving of specific reactions in enzyme-complex reactors.</p>1 aDe, Dinesh1 aDutta, D.1 aKundu, M.1 aMahato, S.1 aSchiavone, M., T.1 aChaudhuri, S.1 aGiri, Ashok, P.1 aGupta, Vidya1 aBhattacharya, S., K.  uhttps://library.ncl.res.in/content/inactive-enzymatic-mutant-proteins-phosphoglycerate-mutase-and-enolase-sugar-binders-102607nas a2200277   4500008004100000022001400041245017500055210006900230260007500299300001400374490000700388520154500395653002001940653001901960653002101979653002802000653002902028100001502057700001902072700002002091700002102111700001802132700002202150700002702172856013002199       2016                        eng d  a0947-653900aVersatile Cu-II metal-organic framework exhibiting high gas storage capacity with selectivity for CO2: conversion of CO2 to cyclic carbonate and other catalytic abilities0 aVersatile CuII metalorganic framework exhibiting high gas storag  aPOSTFACH 101161, 69451 WEINHEIM, GERMANYbWILEY-V C H VERLAG GMBHcMAR  a3387-33960 v223 a<p>A linear tetracarboxylic acid ligand, H4L, with a pendent amine moiety solvothermally forms two isostructural metal-organic frameworks (MOFs) L-M (M=Zn-II, Cu-II). Framework L-Cu can also be obtained from L-Zn by post- synthetic metathesis without losing crystallinity. Compared with L-Zn, the L-Cu framework exhibits high thermal stability and allows removal of guest solvent and metal-bound water molecules to afford the highly porous, L-Cu. At 77K, L-Cu absorbs 2.57wt% of H-2 at 1bar, which increases significantly to 4.67wt% at 36bar. The framework absorbs substantially high amounts of methane (238.38cm(3)g(-1), 17.03wt%) at 303K and 60bar. The CH4 absorption at 303K gives a total volumetric capacity of 166cm(3)(STP)cm(-3) at 35bar (223.25cm(3)g(-1), 15.95wt%). Interestingly, the NH2 groups in the linker, which decorate the channel surface, allow a remarkable 39.0wt% of CO2 to be absorbed at 1bar and 273K, which comes within the dominion of the most famous MOFs for CO2 absorption. Also, L-Cu shows pronounced selectivity for CO2 absorption over CH4, N-2, and H-2 at 273K. The absorbed CO2 can be converted to value-added cyclic carbonates under relatively mild reaction conditions (20bar, 120 degrees C). Finally, L-Cu is found to be an excellent heterogeneous catalyst in regioselective 1,3-dipolar cycloaddition reactions (click reactions) and provides an efficient, economic route for the one-pot synthesis of structurally divergent propargylamines through three-component coupling of alkynes, amines, and aldehydes.</p>10aclick reactions10aCO2 absorption10acyclic carbonate10aheterogeneous catalysis10ametal-organic frameworks1 aDe, Dinesh1 aPal, Tapan, K.1 aNeogi, Subhadip1 aSenthilkumar, S.1 aDas, Debasree1 aGupta, Sayam, Sen1 aBharadwaj, Parimal, K.  uhttps://library.ncl.res.in/content/versatile-cu-ii-metal-organic-framework-exhibiting-high-gas-storage-capacity-selectivity-0