Tekuk Torsi Lateral Balok I Kantilever Non Prismatis

. This paper presents the results of a study about elastic lateral torsional buckling of web tapered cantilever I beams. Elastic buckling analysis was carried out on a number of web tapered cantilever I beam. Beam parameters are expressed in term of dimensionless parameter for lateral torsional buckling and the slope of the side of the tapered web. The analysis is performed using finite element method and the SAP 2000 v 14 program is used to do the analysis. The finite element formulation is based on bifurcation theory. This theory leads to Eigen Value Problem. Critical moment is the lowest Eigen value. The load to be considered is point load at the free end of the beam and uniformly distributed load. Three location of load are considered. The first is at shear center, the second is at top flange and the third is at the bottom flange.From this study, it can be concluded that the slope of the side of tapered web has little influence on the critical moment. But the influence of load height on critical moment is strongly influenced by the slope of the side of the tapered web. Equations for estimating the critical moment has been obtained by regression of the data results of the finite element method

Can Reduction of NO to N₂O in Cytochrome c Dependent Nitric Oxide Reductase Proceed through a Trans-Mechanism?

As part of microbial denitrification, NO is reduced to N₂O in the membrane bound enzyme nitric oxide reductase, NOR. The N–N coupling occurs in the diiron binuclear active site, BNC, and different mechanisms for this reaction step have been suggested. Computational studies have supported a so-called cis:b₃-mechanism, in which the hyponitrite product of the reductive N–N bond formation coordinates with one nitrogen to the heme iron and with both oxygens to the non-heme iron in the BNC. In contrast, experimental results have been interpreted to support a so-called trans-mechanism, in which the hyponitrite intermediate coordinates with one nitrogen atom to each of the two iron ions. Hybrid density functional theory is used here to perform an extensive search for possible intermediates of the NO reduction in the cNOR enzyme. It is found that hyponitrite structures coordinating with their negatively charged oxygens to the positively charged iron ions are the most stable ones. The hyponitrite intermediate involved in the suggested trans-mechanism, which only coordinates with the nitrogens to the iron ions, is found to be prohibitively high in energy, leading to a too slow reaction, which should rule out this mechanism. Furthermore, intermediates binding one NO molecule to each iron ion in the BNC, which have been suggested to initiate the trans-mechanism, are found to be too high in energy to be observable, indicating that the experimentally observed electron paramagnetic resonance signals, taken to support such an iron-nitrosyl dimer intermediate, should be reinterpreted

Energy Diagrams for Water Oxidation in Photosystem II Using Different Density Functionals

The full sequence of intermediates in the water oxidation process in photosystem II has recently been characterized by model calculations, in good agreement with experiments. In the present paper, the energy diagram obtained is used as a benchmark test for several density functionals. Only the results using B3LYP with 15% or 20% show good agreement with experiments. The other functionals tried show errors for some energy levels as large as 20–30 kcal/mol. The reason for these large errors is that the error for three consecutive oxidations of Mn­(III) to Mn­(IV) accumulates as the cluster is oxidized

Mechanism for N₂O Generation in Bacterial Nitric Oxide Reductase: A Quantum Chemical Study

The catalytic mechanism of reduction of NO to N₂O in the bacterial enzyme nitric oxide reductase has been investigated using hybrid density functional theory and a model of the binuclear center (BNC) based on the newly determined crystal structure. The calculations strongly suggest a so-called cis:b₃ mechanism, while the commonly suggested trans mechanism is found to be energetically unfavorable. The mechanism suggested here involves a stable cis-hyponitrite, and it is shown that from this intermediate one N–O bond can be cleaved without the transfer of a proton or an electron into the binuclear active site, in agreement with experimental observations. The fully oxidized intermediate in the catalytic cycle and the resting form of the enzyme are suggested to have an oxo-bridged BNC with two high-spin ferric irons antiferromagnetically coupled. Both steps of reduction of the BNC after N₂O formation are found to be pH-dependent, also in agreement with experiment. Finally, it is found that the oxo bridge in the oxidized BNC can react with NO to give nitrite, which explains the experimental observations that the fully oxidized enzyme reacts with NO, and most likely also the observed substrate inhibition at higher NO concentrations

Hydrolysis of the E2P Phosphoenzyme of the Ca²⁺-ATPase: A Theoretical Study

Dephosphorylation of the E2P phosphoenzyme intermediate of the sarcoplasmic reticulum Ca²⁺-ATPase was studied using density functional theory. The hydrolysis reaction proceeds via a nucleophilic attack on the phosphorylated residue Asp351 by a water molecule, which is positioned by the nearby residue Glu183 acting as a base. The activation barrier was calculated to be 14.3 kcal/mol, which agrees well with values of 15–17 kcal/mol derived from experimentally observed rates. The optimized structure of the transition state reveals considerable bond breakage between phosphorus and the Asp351 oxygen (distance 2.19 Å) and little bond formation to the attacking water oxygen (distance 2.26 Å). Upon formation of the singly protonated phosphate product, Glu183 becomes protonated. The bridging aspartyl phosphate oxygen approaches Lys684 progressively when proceeding from the reactant state (distance 1.94 Å) via the transition state (1.78 Å) to the product state (1.58 Å). This stabilizes the negative charge that develops on the leaving group. The reaction was calculated to be slightly endergonic (+0.9 kcal/mol) and therefore reversible, in line with experimental findings. It is catalyzed by a preorganized active site with little movement of the nonreacting groups except for a rotation of Thr625 toward the phosphate group