A kinetic and thermodynamic study of lac dye adsorption on silk yarn coated with microcrystalline chitosan

The coating of silk yarn with microcrystalline chitosan (MCCh) was carried out using the ultrasonic-assisted method at a pulsed wave frequency of 80 kHz, which only had a slight impact on the yarn as measured by changes in Young\u27s modulus and percentage of elongation compared with untreated silk. A significant enhancement of lac dye uptake onto MCCh-coated silk yarn compared with the untreated silk was observed. The rate of dye uptake at different temperatures onto silk yarn coated with MCCh was investigated. It was found that the adsorption rate constant and diffusion coefficient both increased with increasing temperature, as a result of a diffusion kinetically controlled process with a diffusion activation energy of 9.40 kJ mol −1 . This suggests that dye adsorption on silk yarn coated with MCCh is a physisorption process. The free energy change (∆G ○ ), enthalpy change (∆H ○ ) and entropy change for dye adsorption were also determined, and the negative values of ∆G ○ and ∆H ○ obtained indicated that the lac dye adsorption process is both spontaneous and exothermic

Signal Propagation in the ATPase Domain of Mycobacterium tuberculosis DNA Gyrase from Dynamical-Nonequilibrium Molecular Dynamics Simulations

DNA gyrases catalyze negative supercoiling of DNA, are essential for bacterial DNA replication, transcription, and recombination, and are important antibacterial targets in multiple pathogens, including Mycobacterium tuberculosis, which in 2021 caused &gt;1.5 million deaths worldwide. DNA gyrase is a tetrameric (A 2B 2) protein formed from two subunit types: gyrase A (GyrA) carries the breakage-reunion active site, whereas gyrase B (GyrB) catalyzes ATP hydrolysis required for energy transduction and DNA translocation. The GyrB ATPase domains dimerize in the presence of ATP to trap the translocated DNA (T-DNA) segment as a first step in strand passage, for which hydrolysis of one of the two ATPs and release of the resulting inorganic phosphate is rate-limiting. Here, dynamical-nonequilibrium molecular dynamics (D-NEMD) simulations of the dimeric 43 kDa N-terminal fragment of M. tuberculosis GyrB show how events at the ATPase site (dissociation/hydrolysis of bound nucleotides) are propagated through communication pathways to other functionally important regions of the GyrB ATPase domain. Specifically, our simulations identify two distinct pathways that respectively connect the GyrB ATPase site to the corynebacteria-specific C-loop, thought to interact with GyrA prior to DNA capture, and to the C-terminus of the GyrB transduction domain, which in turn contacts the C-terminal GyrB topoisomerase-primase (TOPRIM) domain responsible for interactions with GyrA and the centrally bound G-segment DNA. The connection between the ATPase site and the C-loop of dimeric GyrB is consistent with the unusual properties of M. tuberculosis DNA gyrase relative to those from other bacterial species. </p