The metal‐catalyzed hydroboration reaction provides access to functionalized organoboron derivatives that cannot be easily prepared using traditional reagents. New developments in this reaction including neoteric reaction media and novel ligands are described in this review. A key aspect of the hydroboration reaction is the ability to further derivatize the product. Thus the conversion of boronate esters into amines, esters, alcohols, carboxylic acids and amino acids is described. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2003)
As benchmarks for judging the catalytic power of sulfate monoesterases, we sought to determine the rates of spontaneous hydrolysis of unactivated alkyl sulfate monoesters by S-O bond cleavage. Neopentyl sulfate proved to be unsuitable for this purpose, since it was found to undergo hydrolysis by a C-O bond cleaving mechanism with rearrangement of its carbon skeleton. Instead, we examined the temperature dependence of the spontaneous hydrolyses of aryl sulfate monoesters, which proceed by S-O cleavage. Extrapolation of a Bronsted plot [log(k(25)(N)) = (-1.81 ± 0.09) pK(a)(LG) + (3.6 ± 0.7)] based on the rate constants at 25 °C for hydrolysis of a series of sulfate monoesters to a pK(a)(LG) value of 16.1, typical of an aliphatic alcohol, yields k(25)(N) = 3 × 10(-26) s(-1). Comparison of that value with established k(cat) values of bacterial sulfatases indicates that these enzymes produce rate enhancements (k(cat)/k(uncat)) of up to 2 × 10(26)-fold for the hydrolysis of sulfate monoesters. These rate enhancements surpass by several orders of magnitude the ~10(21)-fold rate enhancements that are generated by phosphohydrolases, the most powerful biological catalysts previously known. The hydrolytic rates of phosphate and sulfate monoesters are compared directly, and the misleading impression that the two classes of ester are of similar reactivity is dispelled.
Here we show that a recent computationally designed zinc-mediated protein interface is serendipitously capable of catalyzing carboxyester and phosphoester hydrolysis. Although the original motivation was to design a de novo zinc-mediated protein-protein interaction (called MID1-zinc), we observed in the homodimer crystal structure a small cleft and open zinc coordination site. We investigated if the cleft and zinc site at the designed interface were sufficient to form a primitive active site that can perform hydrolysis. MID1-zinc hydrolyzes 4-nitrophenyl acetate (4NPA) with a rate acceleration of 105 and a kcat/KM of 630 M−1s−1, and 4-nitrophenyl phosphate (4NPP) with a rate acceleration of 104 and a kcat/KM of 14 M−1s−1. These rate accelerations by an unoptimized active site highlight the catalytic power of zinc and suggests that the clefts formed by protein-protein interactions are well-suited for creating enzyme active sites. This discovery has implications for protein evolution and engineering: from an evolutionary perspective, 3-coordinated zinc at a homodimer interface cleft represents a simple evolutionary path to nascent enzymatic activity; from a protein engineering perspective, future efforts in de novo design of enzyme active sites may benefit from exploring clefts at protein interfaces for active site placement.
The purpose of this study was to examine force steadiness in three positions of the forearm in young men and women across a variety of force levels. Eight young men and eight young women performed three maximum voluntary contractions (MVCs) in the neutral, supinated, and pronated forearm positions. Viewing a target line on a computer screen, subjects performed submaximal isometric contractions relative to their own MVC at 2.5, 5, 10, 25, 50, and 75% in each of the three forearm positions. Force steadiness was determined as the coefficient of variation (standard deviation around the mean force). A repeated-measures three-way ANOVA was used to assess the differences in force steadiness between sex, position, and force level. Men were stronger than women in all three forearm positions. Overall, men were steadier than women across all force levels and forearm positions. The neutral and supinated positions were equally strong and steady, and the pronated position was the weakest and least steady position. The forearm was most steady between 25 and 75% MVC, and least steady at the lower force levels. When correlations were run between MVC and coefficient of variation at all force levels and all forearm positions, a strong negative relationship was found (r = -0.49). In conclusion, men were stronger, as well as steadier, than women. The neutral and supinated forearm positions were both stronger and steadier than the pronated position. Results suggest that one of the primary factors influencing sex differences in force steadiness is absolute strength.
The Baeyer-Villiger reactions of acetone and 3-pentanone, including their fluorinated and chlorinated derivatives, with performic acid have been studied by ab initio and DFT calculations. Results are compared with experimental findings for the Baeyer-Villiger oxidation of aliphatic fluoro and chloroketones. According to theoretical results, the first transition state is rate-determining for all substrates even in the presence of acid catalyst. Although the introduction of acid into the reaction pathway leads to a dramatic decrease in the activation energy for the first transition state (TS), once entropy is included in the calculations, the enthalpic gain is lost. Of all substrates examined, pentanone reacts with performic acid via the lowest energy transition state. The second transition state is also lowest for pentanone, illustrating the accelerating effect of the additional alkyl group. Interestingly, there is only a small energetic difference in the transition states leading to migration of the fluorinated substituent versus the alkyl substituent in fluoropentanone and fluoroacetone. These differences match remarkably well with the experimentally obtained ratios of oxidation at the fluorinated and nonfluorinated carbons in a series of aliphatic ketones (calculated, 0.3 kcal/mol, observed, 0.5 kcal/mol), which are reported herein. The migration of the chlorinated substituent is significantly more difficult than that of the alkyl, with a difference in the second transition state of approximately 2.6 kcal/mol.
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