Journal of Biological Inorganic Chemistry最新文献

{"title":"Author Correction: Evaluation of Au(III) complexes as Plasmodium falciparum aquaglyceroporin (PfAQP) inhibitors by in silico and in vitro methods","authors":"Federico Balgera, Muyideen Kolapo Tijani, Johan Wennerberg, Kristina E. M. Persson, Ebbe Nordlander, Ricardo J. Ferreira","doi":"10.1007/s00775-025-02108-x","DOIUrl":"10.1007/s00775-025-02108-x","url":null,"abstract":"","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 3","pages":"311 - 311"},"PeriodicalIF":2.7,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143612889","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bismuth(III) complexes of Schiff bases derived from aliphatic amines: interaction with biomolecules and antimicrobial activity","authors":"Maxim Gvozdev,&nbsp;Iveta Turomsha,&nbsp;Nikolai Osipovich,&nbsp;Galina Ksendzova,&nbsp;Alina Khodosovskaya,&nbsp;Anton Siomchen,&nbsp;Janusz M. Dąbrowski,&nbsp;Natalia Loginova","doi":"10.1007/s00775-025-02107-y","DOIUrl":"10.1007/s00775-025-02107-y","url":null,"abstract":"<div><p>Schiff bases bearing a sterically hindered phenolic moiety and their Bi(III) complexes were synthesized and characterized by physicochemical, quantum chemical, and biological methods. The compounds were screened in vitro against bacterial and yeast strains. It was found that Bi(III) complexes demonstrate higher antimicrobial activity compared to the parent ligands as well as to the commonly used drug (De-Nol®). Moreover, the antibacterial activity of investigated compounds did not directly correlate with their hemolytic activity, indicating that the antimicrobial effect of Bi(III) complexes cannot be explained solely by their membranolytic properties. Spectrofluorometric studies of the interaction of the Bi(III) complexes with plasma proteins indicate their moderate to high affinity toward BSA and hemoglobin, which is crucial for the determination of their pharmacological profile as well as toxicity assessment. Additionally, molecular docking was performed to predict the possible interaction modes and binding energies of the tested compounds at the molecular level. The results obtained may provide the basis for the design and development of novel Bi(III)-based antimicrobial agents.</p><h3>Graphical abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 3","pages":"257 - 269"},"PeriodicalIF":2.7,"publicationDate":"2025-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143582153","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Crystal structure of ferric recombinant horseradish peroxidase","authors":"Mst Luthfun Nesa,&nbsp;Suman K. Mandal,&nbsp;Christine Toelzer,&nbsp;Diana Humer,&nbsp;Peter C. E. Moody,&nbsp;Imre Berger,&nbsp;Oliver Spadiut,&nbsp;Emma L. Raven","doi":"10.1007/s00775-025-02103-2","DOIUrl":"10.1007/s00775-025-02103-2","url":null,"abstract":"<div><p>Horseradish peroxidase (HRP), isolated from horseradish roots, is heavily glycosylated, making it difficult to crystallize. In this work, we produced recombinant HRP in <i>E. coli</i> and obtained an X-ray structure of the ferric enzyme at 1.63 Å resolution. The structure shows that the recombinant HRP contains four disulphide bonds and two calcium ions, which are highly conserved in class III peroxidase enzymes. The heme active site contains histidine residues at the proximal (His 170) and distal (His 42) positions, and an active site arginine (Arg 38). Surprisingly, an ethylene glycol molecule was identified in the active site, forming hydrogen bonds with His 42 and Arg 38 at the δ-heme edge. The high yields obtained from the recombinant expression system, and the successful crystallization of the enzyme pave the way for new structural studies in the future.</p><h3>Graphical abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 3","pages":"221 - 227"},"PeriodicalIF":2.7,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-025-02103-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143571909","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Extending protein-film electrochemistry across enzymology and biological inorganic chemistry to investigate, track and control the reactions of non-redox enzymes and spectroscopically silent metals","authors":"Clare F. Megarity,&nbsp;Ryan A. Herold,&nbsp;Fraser A. Armstrong","doi":"10.1007/s00775-025-02105-0","DOIUrl":"10.1007/s00775-025-02105-0","url":null,"abstract":"<div><p>Protein film electrochemistry has helped to unravel many complex reactivities of electron-transferring proteins and enzymes. A versatile descendant, the ‘Electrochemical Leaf’, offers new opportunities to extend electrochemical control to myriad enzymes that neither transfer electrons nor catalyse any redox reaction, including those dependent on spectroscopically limited, labile or other challenging metal ions. By embedding a cascade comprised of several enzymes—one of which electrochemically recycles NAD(P)(H), a second being a dehydrogenase—within a porous electrode formed from fused nanoparticles, the interconnected reactions are tightly channeled to transmit energy and information, rapidly and interactively. Under nanoconfinement, nicotinamide cofactors and cascade intermediates serve as specific current carriers, far beyond the electron itself.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 3","pages":"209 - 219"},"PeriodicalIF":2.7,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-025-02105-0.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143536320","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editorial by the Chief Editor","authors":"Nils Metzler-Nolte","doi":"10.1007/s00775-025-02104-1","DOIUrl":"10.1007/s00775-025-02104-1","url":null,"abstract":"","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 1","pages":"1 - 2"},"PeriodicalIF":2.7,"publicationDate":"2025-02-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-025-02104-1.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143514308","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cytochromes P460 and c′-β: exploiting a novel fold for multiple functions","authors":"Hannah R. Adams,&nbsp;Sotaro Fujii,&nbsp;Hans E. Pfalzgraf,&nbsp;Peter Smyth,&nbsp;Colin R. Andrew,&nbsp;Michael A. Hough","doi":"10.1007/s00775-025-02102-3","DOIUrl":"10.1007/s00775-025-02102-3","url":null,"abstract":"<div><p>Two related classes of ligand-binding heme <i>c</i>-containing proteins with a high degree of structural homology have been identified and characterized over recent decades: cytochromes P460 (cyts P460), defined by an unusual heme-lysine cross-link, and cytochromes <i>c</i>′-β (cyts <i>c</i>′-β), containing a canonical <i>c</i>-heme without the lysine cross-link. The shared protein fold of the cyt P460-cyt <i>c</i>′-β superfamily can accommodate a variety of heme environments with entirely different reactivities. On the one hand, cyts P460 with polar distal pockets have been shown to oxidize NH₂OH to NO and/or N₂O via proton-coupled electron transfer. On the other hand, cyts <i>c</i>′-β with hydrophobic distal pockets have a proposed gas binding function similar to the unrelated, but more extensively characterized, alpha helical cytochromes <i>c</i>′. Recent studies have also identified ‘halfway house’ proteins (cyts P460 with non-polar heme pockets and cyts <i>c</i>′-β with polar distal heme pockets) with functions yet to be resolved. Here, we review the structural, spectroscopic and enzymatic properties of the cyt P460-cyt <i>c</i>′-β superfamily with a view to understanding the structural determinants of their different functional properties.</p><h3>Graphical abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 2","pages":"181 - 207"},"PeriodicalIF":2.7,"publicationDate":"2025-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-025-02102-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143497719","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Copper-chelating natural products","authors":"Olivia M. Manley,&nbsp;Amy C. Rosenzweig","doi":"10.1007/s00775-025-02099-9","DOIUrl":"10.1007/s00775-025-02099-9","url":null,"abstract":"<div><p>Bacteria and fungi produce natural products that coordinate copper for a variety of functions. Many copper-binding natural products function as copper-chelating metallophores, or chalkophores, that scavenge copper from the environment to meet cellular needs. By contrast, some compounds sequester toxic levels of environmental copper to protect the producing microorganism. These copper-binding compounds often have antimicrobial activities as well. In recent years, a number of new copper-coordinating natural products have been reported, including both ribosomally and non-ribosomally synthesized molecules. There have also been significant advances in understanding the biosynthesis of these and previously known copper chelators, leading to the discovery of new enzyme families. This review summarizes the recently discovered copper-binding natural products, their biosynthetic pathways, and their functions. By highlighting key biosynthetic enzymes, we hope to inspire the discovery of new copper-coordinating natural products that may be used as therapeutics and antimicrobial agents.</p><h3>Graphical abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 2","pages":"111 - 124"},"PeriodicalIF":2.7,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143439686","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of the substrate specificity and regioselectivity of ring-cleavage of Pseudomonas putida DLL-E4 hydroquinone 1,2-dioxygenase (PnpC1C2)","authors":"Timothy E. Machonkin,&nbsp;Madeleine S. Maker,&nbsp;Nandin Ganjoloo,&nbsp;Drew F. Conkin","doi":"10.1007/s00775-025-02101-4","DOIUrl":"10.1007/s00775-025-02101-4","url":null,"abstract":"<div><p>PnpC1C2 is an enzyme from the soil bacterium <i>Pseudomonas putida</i> DLL-E4 that is in the pathway for the oxidative catabolism of 4-nitrophenol. PnpC1C2 oxidatively cleaves hydroquinone into γ-hydroxymuconic semialdehyde. It belongs to the type II hydroquinone dioxygenase family, a relatively uncharacterized group of mononuclear non-heme Fe(II)-dependent enzymes that catalyze oxidative ring-cleavage reactions, which includes the well-studied catechol extradiol dioxygenases as well as the structurally unrelated 2,6-dichlorohydroquinone dioxygenase (PcpA). Steady-state kinetics studies using UV/Vis spectroscopy were performed to characterize the enzyme specificity towards various substituted hydroquinones. In addition to its native substrate, PnpC1C2 was active towards a variety of monosubstituted hydroquinones. Methyl- and methoxyhydroquinone showed a moderately higher <span>(K_{mA}^{app})</span>, and chloro- and bromohydroquinone showed a moderately lower <span>(k_{cat}^{app})</span>, but all had a <span>({{k_{cat}^{app} } mathord{left/ {vphantom {{k_{cat}^{app} } {K_{mA}^{app} }}} right. kern-0pt} {K_{mA}^{app} }})</span> within an order of magnitude of unsubstituted hydroquinone. Likewise, only small differences in the rates of mechanism-based inactivation were observed among these substrates. Among disubstituted hydroquinones, only 2,6- and 2,5-dimethylhydroquinone showed any activity, with the latter only barely detectable. A variety of <i>para</i>-substituted phenols were found to be good inhibitors of PnpC1C2. NMR studies were performed to determine the regioselectivity of ring-cleavage with monosubstituted hydroquinones. All monosubstituted hydroquinones tested (methyl-, chloro-, bromo-, and methoxyhydroquinone) yielded exclusively the 1,6-cleavage product. Thus, PnpC1C2 shows notable differences in both its substrate specificity and the ring-cleavage regioselectivity compared to that of PcpA. These results provide an important basis for future comparison of structure–function correlations among the hydroquinone ring-cleaving dioxygenases.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 1","pages":"35 - 51"},"PeriodicalIF":2.7,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143439685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The chlorite adduct of aquacobalamin: contrast with chlorite dismutase","authors":"Maria Lehene,&nbsp;Cezara Zagrean-Tuza,&nbsp;Stefania D. Iancu,&nbsp;Sergiu-Raul Cosma,&nbsp;Adrian M. V. Brânzanic,&nbsp;Radu Silaghi-Dumitrescu,&nbsp;Bianca Stoean","doi":"10.1007/s00775-025-02100-5","DOIUrl":"10.1007/s00775-025-02100-5","url":null,"abstract":"<div><p>In the reaction of aquacobalamin (aquaCbl) with chlorite, a stable species is detected and assigned as a Co(III)–chlorite complex, Co(III)–OClO⁻. Its UV–Vis spectrum is almost identical to that of aquaCbl, except for some minor differences at ~ 430 nm; cyanide can eliminate and prevent these changes. The ¹H-NMR spectra reveal strong influences of chlorite on the B2 and B4 protons of the cobalt-bound dimethyl benzimidazole ligand. Together, the UV–Vis and NMR titrations suggest a Kd of 10 mM or higher for chlorite on Cbl. Resonance Raman spectra reveal minor changes in the spectrum of aquaCbl to chlorite—as well as a disappearance of the free chlorite signals, consistent with Cbl–chlorite complex formation. Corroboration for these interpretations is also offered from mass spectrometry and DFT calculations. This Co(III)–OClO⁻ complex would be a stable analogue of the first reaction intermediate in the catalytic cycle of chlorite dismutase, or in the reaction of chlorite with a number of other heme proteins. The differences in reactivity between Co(III) cobalamin and Fe(III) heme towards chlorite are analyzed and rationalized, leading to a reconciliation of experimental and computational data for the latter.</p></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 1","pages":"25 - 34"},"PeriodicalIF":2.7,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-025-02100-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143373715","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Donut-shaped [NaP5W30O110]14− polyoxometalate as a promising antidiabetic drug-candidate: putative mechanisms of action","authors":"Marko Dinčić,&nbsp;Mirjana B. Čolović,&nbsp;Jasna Todorović,&nbsp;Neda Milinković,&nbsp;Branimir Radosavljević,&nbsp;Ali S. Mougharbel,&nbsp;Ulrich Kortz,&nbsp;Danijela Z. Krstić","doi":"10.1007/s00775-025-02098-w","DOIUrl":"10.1007/s00775-025-02098-w","url":null,"abstract":"<div><p>The aim of this study was to elucidate the potential mechanism of the antihyperglycemic action of the donut-shaped Preyssler-Pope-Jeannin polyanion salt (NH₄)₁₄[NaP₅W₃₀O₁₁₀] 31H₂O (<b>NaP</b>_<b>5</b><b>W</b>_<b>30</b>) and its effect on metabolic disorders associated with diabetes. For this purpose, relevant parameters of blood glucose regulation, lipid profile, and electrolyte status were monitored in streptozotocin (STZ)-induced diabetic rats that were orally treated with 20 mg/kg/day <b>NaP</b>_<b>5</b><b>W</b>_<b>30</b> for three weeks. The serum insulin concentration was increased in diabetic animals treated with <b>NaP</b>_<b>5</b><b>W</b>_<b>30</b> (20 mg/kg/day, per os, three weeks), which could be one of the possible mechanisms of the confirmed antihyperglycemic effect. In addition, the administration of <b>NaP</b>_<b>5</b><b>W</b>_<b>30</b> significantly reduced hyperglycemia and glycated haemoglobin A_1c (HbA_1c) in STZ-induced diabetic rats, although normoglycemic values were not achieved. Furthermore, a statistically significant 1.3-fold reduction in serum total cholesterol and a 1.7-fold reduction in high-density lipoprotein (HDL) cholesterol were observed in the <b>NaP</b>_<b>5</b><b>W</b>_<b>30</b> treatment group compared to the diabetic control group. In contrast, <b>NaP</b>_<b>5</b><b>W</b>_<b>30</b> had no effect on homeostasis model assessment of insulin resistance (HOMA-IR) index values, electrolyte concentrations, or serum concentrations of low-density lipoprotein (LDL) cholesterol, apolipoprotein A1 (Apo A1), apolipoprotein B (Apo B), or total triglycerides. In summary, <b>NaP</b>_<b>5</b><b>W</b>_<b>30</b> effectively improved glycoregulation in diabetic rats via the considerable stimulation of insulin as a putative mechanism. Moreover, <b>NaP</b>_<b>5</b><b>W</b>_<b>30</b> did not affect rat weight or disrupt lipid and electrolyte status, common diabetes-followed side effects and risk factors for various life-threatening complications. Thus, <b>NaP</b>_<b>5</b><b>W</b>_<b>30</b> could be considered a promising antidiabetic drug-candidate that deserves further investigation.</p><h3>Graphical abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 3","pages":"283 - 298"},"PeriodicalIF":2.7,"publicationDate":"2025-02-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143254333","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}