Student-Invented Numeration Systems: Pattern-Analysis and Mathematical Understanding

Thirteen fifth graders were given an assignment to invent their own numeration systems, following a unit on bases and a look at early events in the history of numbers. The task presented options that required the students to make decisions (such as whether to use a base, which base to use, design of symbols, etc.), and build a rationale for the elements of their system. Analyses of patterns embedded in their invented systems provided an assessment of student understanding of numeration. The progression of more and less complex thinking related to the student's choice of a base other than 10, consistency of logic throughout the system in words and symbols, rationale for change, and perception of real life examples that would change if the system was adopted. The invention task is presented as another way to make connections.     

CHLORINATION OF ISOLATED CHLOROPHYLLS in vitro

Abstract— It was shown that chlorophyll a and its epimer chlorophyll a' are chlorinated and hydroxyl-ated during thin layer chromatography with silica gel plates. Hydroxylated chlorophyll a could not be chlorinated. Chlorinated and non chlorinated chlorophylls could be separated and determined by high performance liquid chromatography, because chlorophylls do not alter during this procedure. These findings support the assumption that Chi RC I is a preparation artifact. The extent of chlorination depends on chloride availability on the thin layer and on time. Chlorination and hydroyxlation do not take place under nitrogen atmosphere. The mechanism of chlorination during the thin layer chromatography procedure is discussed.     

Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture

[FeFe]-hydrogenases are known for their high rates of hydrogen turnover, and are intensively studied in the context of biotechnological applications. Evolution has generated a plethora of different subclasses with widely different characteristics. The M2e subclass is phylogenetically distinct from previously characterized members of this enzyme family and its biological role is unknown. It features significant differences in domain- and active site architecture, and is most closely related to the putative sensory [FeFe]-hydrogenases. Here we report the first comprehensive biochemical and spectroscopical characterization of an M2e enzyme, derived from Thermoanaerobacter mathranii. As compared to other [FeFe]-hydrogenases characterized to-date, this enzyme displays an increased H₂ affinity, higher activation enthalpies for H⁺/H₂ interconversion, and unusual reactivity towards known hydrogenase inhibitors. These properties are related to differences in active site architecture between the M2e [FeFe]-hydrogenase and “prototypical” [FeFe]-hydrogenases. Thus, this study provides new insight into the role of this subclass in hydrogen metabolism and the influence of the active site pocket on the chemistry of the H-cluster.

Characterization of a group D putative sensory [FeFe]-hydrogenase reveals how the active site can be tuned to decrease CO inhibition and increase stability of a reduced H-cluster while retaining the ability to catalyze H⁺/H₂ interconversion.