Treating [Ru(PPh₃)₃Cl₂] with the amine 2-picolylamine (Picam) ligand in a 1:1 molar ratio, the Ru(II) complex trans-Ru(PPh₃)₂(Picam)Cl₂ (1) is obtained in methylene chloride and can be isolated as a pure solid compound. The single-crystal structure of 1 was determined by X-ray crystallography. The geometry at the Ru metal center is a distorted octahedral environment with a trans arrangement of the two chlorides. A trans effect of the bond lengths was observed within the structure. Similarly, treating [Ru(PPh₃)₃Cl₂] with 1:1:1 molar ratios of 2-picolylamine (Picam) and 1,1′-bis(diphenylphosphine)ferrocene (DPPF) ligands yielded the Ru(II) complex trans-Ru(DPPF)(Picam)Cl₂ (2). In identical conditions, the homogeneous hydrogen transfer catalytic reactivity of complexes 1 and 2 has been tested in a basic 2-propanol solution and they indicate different catalytic activity. It was discovered that monodentate and bidentate phosphine ligands of Ru(II) complexes, as well as cis- and trans-chloro configuration display different catalytic properties from our experimental data, in agreement with literature data. Based on DFT calculations, the relative molecular catalytic reactivity of all available experimental data is understood from the relative calculated molecular energy.

Three oxygen donor gallium(III) halide complexes, [GaX₃(O=P(TMP)₃] (TMP = trimethoxylphenyl and X = Cl⁻ (1), Br⁻ (2) and I⁻ (3)), are prepared by oxidation in mixed solvents from their phosphine adducts of [GaX₃(P(TMP)₃]. Three crystalline compounds are obtained from the solutions and their crystal structures are determined in the solid state. It is rare to generate a crystalline phase for metal–adduct compounds of this bulky ligand; in this paper, three new crystal structures are presented.

Green chemistry, achieved by using water as a reaction medium, has several potential applications. In this work, a number of water-soluble Rh(III)–THP complexes, [Rh(III)Cl₃(OH)(THP)₂]⁻ (1), [Rh(III)Cl₂(OH)(THP)₃] (2), [Rh(III)Cl(OH)(THP)₄]⁺ (3), [Rh(III)Cl(OH)(en)(THP)₂]⁺ (4a), [Rh(I)(en)(THP)₂]⁺ (4b) and [Rh(III)(en)₂Cl₂]Cl (5) (where THP = P(CH₂OH)₃), were generated in aqueous media by controlling the reaction at different molar ratios of RhCl₃/THP/en (en: ethylenediamine). These complexes were fully characterized in situ by ³¹P NMR spectroscopy, base titration and by X-ray crystallography for the solid compound (4). The catalytic hydrogenation reactivities of freshly prepared complexes (1–5) were tested in situ with the selected substrate of 3,4-dimethoxystyrene under the same experimental conditions; the related catalytic reactivities are discussed in detail.

Introduction: Mycobacterium tuberculosis in natural environments and host organisms must adapt to constantly changing growth conditions, and its adaptive mechanism for nutrient metabolism represents one response to complex environments. Reversible post-translational protein modifications regulate central metabolic enzymes in M. tuberculosis , thereby governing its adaptation to varying environmental nutrient availability. Methods: In this study, we cultured Mycobacterium smegmatis MC ² 155 using Sauton or Middlebrook 7H9 media and applied liquid chromatography–tandem mass spectrometry (LC–MS/MS) to analyze differences in acetylation-modified proteins. We also performed bioinformatic analysis of the acetylated proteins expressed in the different media. Results: LC–MS/MS revealed 182 acetylated proteins and 398 sites exclusively in Sauton-medium-cultured strains; whereas 57 acetylated proteins and 141 sites were identified exclusively in nutrient-rich 7H9-medium-cultured strains. Additionally, 302 proteins and 462 sites were differentially acetylated between the Sauton- and 7H9-medium-cultured samples. Our bioinformatics analysis identified differences in whole-protein acetylation modifications in M. smegmatis MC ² 155 under these two culture conditions, primarily reflected in metabolic pathways, including the citrate cycle (TCA cycle), 2-oxocarboxylic acid metabolism, carbon metabolism, RNA degradation, and tryptophan metabolism. Discussion: Under the nutrient-limited conditions of Sauton medium culture, multiple sites within isocitrate dehydrogenase exhibited acetylation, leading to reduced enzyme activity. This effect may redirect a greater proportion of carbon flux towards the glyoxylate pathway. Conversely, in 7H9 medium, acetylation at residues K189 and K331 of isocitrate lyase may diminish enzyme activity, thereby channeling increased carbon flux towards the TCA cycle. Acetylation at 3-hydroxyacyl-CoA dehydrogenase (K370) and tryptophan-tRNA synthetase (K200) may reduce fatty acid and protein synthesis, thereby preventing excessive energy expenditure; acetylation at Oligoribonuclease K153 likely diminishes enzyme activity, thereby allowing M. smegmatis to adapt to nutrient limitation by accumulating more c-di-AMP.