Journal of Inorganic Biochemistry最新文献

{"title":"Expanding the scope of resonance Raman spectroscopy in hydrogenase research: New observable states and reporter vibrations","authors":"Cornelius C.M. Bernitzky ,&nbsp;Giorgio Caserta ,&nbsp;Stefan Frielingsdorf ,&nbsp;Janna Schoknecht ,&nbsp;Andrea Schmidt ,&nbsp;Patrick Scheerer ,&nbsp;Oliver Lenz ,&nbsp;Peter Hildebrandt ,&nbsp;Christian Lorent ,&nbsp;Ingo Zebger ,&nbsp;Marius Horch","doi":"10.1016/j.jinorgbio.2024.112741","DOIUrl":"10.1016/j.jinorgbio.2024.112741","url":null,"abstract":"<div><div>Oxygen-tolerant [NiFe] hydrogenases are valuable blueprints for the activation and evolution of molecular hydrogen under application-relevant conditions. Vibrational spectroscopic techniques play a key role in the investigation of these metalloenzymes. For instance, resonance Raman spectroscopy has been introduced as a site-selective approach for probing metal-ligand coordinates of the [NiFe] active site and FeS clusters. Despite its success, this approach is still challenged by a limited number of detectable active-site states – due to missing resonance enhancement or intrinsic light sensitivity – and difficulties in their assignment. Utilizing two oxygen-tolerant [NiFe] hydrogenases as model systems, we illustrate how these challenges can be met by extending excitation and detection wavelength regimes in resonance Raman spectroscopic studies. Specifically, we observe that this technique does not only probe low-frequency metal-ligand vibrations but also high-frequency intra-ligand modes of the diatomic CO/CN⁻ ligands at the active site of [NiFe] hydrogenases. These reporter vibrations are routinely probed by infrared absorption spectroscopy, so that direct comparison of spectra from both techniques allows an unambiguous assignment of states detected by resonance Raman spectroscopy. Moreover, we find that a previously undetected state featuring a bridging hydroxo ligand between Ni and Fe can be probed using higher excitation wavelengths, as photoconversion occurring at lower wavelengths is avoided. In summary, this study expands the applicability of resonance Raman spectroscopy to hydrogenases and other complex metalloenzymes by introducing new strategies for probing and assigning redox-structural states of the active site.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112741"},"PeriodicalIF":3.8,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142320357","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"EcNikA, a versatile tool in the field of artificial metalloenzymes","authors":"Caroline Marchi-Delapierre,&nbsp;Christine Cavazza,&nbsp;Stéphane Ménage","doi":"10.1016/j.jinorgbio.2024.112740","DOIUrl":"10.1016/j.jinorgbio.2024.112740","url":null,"abstract":"<div><div>This review describes the multiple advantages of using of <em>Ec</em>NikA, a nickel transport protein, in the design of artificial metalloenzymes as alternative catalysts for synthetic biology. The rationale behind the strategy of artificial enzyme design is discussed, with particular emphasis on <em>de novo</em> active site reconstitution. The impact of the protein scaffold on the artificial active site and thus the final catalytic properties is detailed, highlighting the considerable aptitude of hybrid systems to catalyze selective reactions, from alkene to thioether transformations (epoxidation, hydroxychlorination, sulfoxidation). The different catalytic approaches – from <em>in vitro</em> to <em>in cristallo</em> – are compared, revealing the considerable advantages of protein crystals in terms of stabilization and acceleration of reaction kinetics. The versatility of proteins, based on metal and ligand diversity and medium/physical conditions, are thus illustrated for oxidation catalysis.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112740"},"PeriodicalIF":3.8,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142454989","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis, characterization and comparative biological activity of a novel set of Cu(II) complexes containing azole-based ligand frames","authors":"Courtney E. Elwell ,&nbsp;Emily Stein ,&nbsp;Adam Lewis ,&nbsp;Stefan Hamaway ,&nbsp;Kennedy A. Alexis ,&nbsp;Joseph M. Tanski ,&nbsp;Timothy J. Barnum ,&nbsp;Colleen M. Connelly ,&nbsp;Laurie A. Tyler","doi":"10.1016/j.jinorgbio.2024.112736","DOIUrl":"10.1016/j.jinorgbio.2024.112736","url":null,"abstract":"<div><div>The synthesis and spectroscopic characterization of three complexes containing a substituted 2-(2-pyridyl)benzothiazole (PyBTh) group in the ligand frame are reported along with the comparative biological activity. The ligands have been substituted at the 6-position with either a methoxy (Py(<em>OMe</em>)BTh) or a methyl group (Py(<em>Me</em>)BTh). Reaction of Py(<em>OMe</em>)BTh with either CuCl₂ or Cu(NO₃)₂·2.5 H₂O yielded the monomeric [Cu(Py(<em>OMe</em>)BTh))₂(NO₃)]NO₃·1.5 MeOH, (<strong>1</strong>·1.5 MeOH) complex or the dimeric [Cu(Py(<em>OMe</em>)BTh)Cl₂]₂ (<strong>2</strong>), respectively, with the nuclearity of the complex dependent on the starting Cu(II) salt. Reaction between the methyl substituted ligand and Cu(NO₃)₂·2.5 H₂O resulted in the isolation of Cu(Py(<em>Me</em>)BTh)(NO₃)₂·0.5 THF (<strong>3</strong>·0.5 THF). Complexes <strong>1</strong>–<strong>3</strong> were fully characterized. Cyclic voltammetry measurements were performed on all three complexes as well as on [Cu(PyBTh)₂(H₂O)](BF₄)₂ (<strong>4</strong>), a compound previously reported by us which contains the unsubstituted 2-(2-pyridyl)benzothiazole ligand. The biological activity was studied and included concentration dependent DNA binding and cleavage, antibacterial activity, and cancer cell toxicity. All complexes exhibited DNA cleavage activity, however <strong>2</strong> and <strong>4</strong> were found to be the most potent. Mechanistic studies revealed that the nuclease activity is dependent on an oxidative mechanism reliant principally on O₂⁻. Antibacterial studies revealed complex <strong>4</strong> was more potent compared to <strong>1</strong>–<strong>3</strong>. Cancer cell toxicity studies were carried out on HeLa, PC-3, and MCF7 cells with <strong>1</strong>–<strong>4</strong>, Cu(QBTh)(NO₃)₂(H₂O) and Cu(PyBIm)₃(BF₄)₂. The differences in the observed toxicities suggests the importance of the ligand and its substituents in modulating cell death.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112736"},"PeriodicalIF":3.8,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142322293","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mononuclear high-spin iron(III) phthalocyanines","authors":"Yusuke Okada,&nbsp;Nagao Kobayashi","doi":"10.1016/j.jinorgbio.2024.112737","DOIUrl":"10.1016/j.jinorgbio.2024.112737","url":null,"abstract":"<div><div>2,9(or 10),16(or 17), 23(or 24)-Tetradecyloxycarbonylphthalocyaninatoiron, FeTDPc, and 2,3,9,10,16,17,23,24-octadecyloxycarbonylphthalocyaninatoiron, FeODPc, were synthesized and characterized. These compounds seem to be in trivalent iron high-spin state in solvents such as chloroform, dichloromethane, benzene, and chlorobenzene, although their counter anion could not be detected by elemental analyses. They react with strong bases such as pyridine and imidazoles to form their mono- and subsequently their di-base complexes with formation constant of &gt;10⁶ and &lt; 200 dm³ mol⁻¹, respectively, in dichloromethane at 20 °C. The resultant mono-adducts appear to be trivalent iron low-spin while the di-base adducts are bivalent iron low-spin state complexes. The addition of ca. 10–30 equivalent of tetrabutylammonium-chloride or -bromide (electrolyte) to the solution containing FeTDPc or FeODPc, causes their spin-state change from iron(III) high to low-spin state. In a solid power state, however, both FeTDPc and FeODPc exist as a mixture of high-spin iron(III)- and intermediate-spin iron(II) species. Strangely, when these compounds are dissolved in polystyrene, i.e. each molecules are isolated from each other, the signals originated from the iron(II) component disappear.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112737"},"PeriodicalIF":3.8,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142314594","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Exploiting the potential of rivastigmine-melatonin derivatives as multitarget metal-modulating drugs for neurodegenerative diseases","authors":"Inês Dias ,&nbsp;Leo Bon ,&nbsp;Angelika Banas` ,&nbsp;Daniel Chavarria ,&nbsp;Fernanda Borges ,&nbsp;Catarina Guerreiro-Oliveira ,&nbsp;Sandra M. Cardoso ,&nbsp;Daniele Sanna ,&nbsp;Eugenio Garribba ,&nbsp;Sílvia Chaves ,&nbsp;M. Amélia Santos","doi":"10.1016/j.jinorgbio.2024.112734","DOIUrl":"10.1016/j.jinorgbio.2024.112734","url":null,"abstract":"<div><div>The multifaceted nature of the neurodegenerative diseases, as Alzheimer's disease (AD) and Parkinson's disease (PD) with several interconnected etiologies, and the absence of effective drugs, led herein to the development and study of a series of multi-target directed ligands (MTDLs). The developed RIV-IND hybrids, derived from the conjugation of an approved anti-AD drug, rivastigmine (RIV), with melatonin analogues, namely indole (IND) derivatives, revealed multifunctional properties, by associating the cholinesterase inhibition of the RIV drug with antioxidant activity, biometal (Cu(II), Zn(II), Fe(III)) chelation properties, inhibition of amyloid-<em>β</em> (A<em>β</em>) aggregation (self- and Cu-induced) and of monoamine oxidases (MAOs), as well as neuroprotection capacity in cell models of AD and PD. In particular, two hybrids with hydroxyl-substituted indoles (<strong>5a2</strong> and <strong>5a3</strong>) could be promising multifunctional compounds that inspire further development of novel anti-neurodegenerative drugs.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112734"},"PeriodicalIF":3.8,"publicationDate":"2024-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142387006","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Polyoxometalates and their composites for antimicrobial applications: Advances, mechanisms and future prospects","authors":"Min Ma ,&nbsp;Jiayin Chen ,&nbsp;Liuyang Dong ,&nbsp;Yue Su ,&nbsp;Shufang Tian ,&nbsp;Yuemin Zhou ,&nbsp;Mingxue Li","doi":"10.1016/j.jinorgbio.2024.112739","DOIUrl":"10.1016/j.jinorgbio.2024.112739","url":null,"abstract":"<div><p>The overuse of antibiotics can lead to the development of antibiotic-resistant bacteria, which can be even more difficult to treat and pose an even greater threat to public health. In order to address the issue of antibiotic-resistant bacteria, researchers currently are exploring alternative methods of sterilization that are both effective and sustainable. Polyoxometalates (POMs), as emerging transition metal oxide compounds, exhibit significant potential in various applications due to their remarkable tunable physical and chemical performance, especially in antibacterial fields. They constitute a diverse family of inorganic clusters, characterized by a wide array of composition, structures and charges. Presently, several studies indicated that POM-based composites have garnered extensive attention in the realms of the antibacterial field and may become promising materials for future medical applications. Moreover, this review will focus on exploring the antibacterial properties and mechanisms of different kinds of organic-inorganic hybrid POMs, POM-based composites, films and hydrogels with substantial bioactivity, while POM-based composites have the dual advantages of POMs and other materials. Additionally, the potential antimicrobial mechanisms have also been discussed, mainly encompassing cell wall/membrane disruption, intracellular material leakage, heightened intracellular reactive oxygen species (ROS) levels, and depletion of glutathione (GSH). These findings open up exciting possibilities for POMs as exemplary materials in the antibacterial arena and expand their prospective applications.</p></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112739"},"PeriodicalIF":3.8,"publicationDate":"2024-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142243102","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Construction of artificial peroxidase based on myoglobin scaffold for efficient degradation of meloxicam","authors":"Weikang Zhang ,&nbsp;Yadan Yang ,&nbsp;Xiangmin Meng ,&nbsp;Fang Wang ,&nbsp;Ying-Wu Lin ,&nbsp;Jiakun Xu","doi":"10.1016/j.jinorgbio.2024.112733","DOIUrl":"10.1016/j.jinorgbio.2024.112733","url":null,"abstract":"<div><p>A novel artificial peroxidase has been developed for the efficient degradation of the non-steroidal anti-inflammatory drug meloxicam by combining computer simulation and genetic engineering techniques. The results showed that the artificial peroxidase was able to completely degrade meloxicam within 90 s, with a degradation rate of 100 %, which was much higher than that of natural lacquer (46 %). The reaction time of the artificial enzyme was significantly shorter than that of natural peroxidase (10 min) and laccase (48 h). Further studies showed that the amino acid arrangement of the active site of the protein plays an important role in the catalytic performance. The degradation pathway of meloxicam was revealed using UPLC-MS analysis. In vitro toxicity assay showed complete disappearance of toxicity after meloxicam degradation. Therefore, the biocatalytic system proved to be an effective route for the green degradation of meloxicam with important application potential.</p></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112733"},"PeriodicalIF":3.8,"publicationDate":"2024-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142243103","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In(III) pyridinecarboxylate complexes: Composition, solution equilibria estimation, bioevaluation and interactions with HSA","authors":"Michaela Rendošová ,&nbsp;Róbert Gyepes ,&nbsp;Adrián Gucký ,&nbsp;Mária Kožurková ,&nbsp;Mária Vilková ,&nbsp;Petra Olejníková ,&nbsp;Martin Kello ,&nbsp;Alan Liška ,&nbsp;Ivana Kléri ,&nbsp;Jana Havlíčková ,&nbsp;Adrián Tamáš ,&nbsp;Zuzana Vargová","doi":"10.1016/j.jinorgbio.2024.112738","DOIUrl":"10.1016/j.jinorgbio.2024.112738","url":null,"abstract":"<div><p>Two In(III) – pyridinecarboxylates ([In(Pic)₂(NO₃)(H₂O)] (InPic; HPic = picolinic acid), [In(HDpic)(Dpic)(H₂O)₂]·5H₂O (InDpic; H₂Dpic = dipicolinic acid), have been synthesized by one-step procedure. The complexes composition was confirmed by physicochemical analyses and X-ray diffraction confirmed molecular structure of both complexes. Moreover, complex species speciation was described in both systems by potentiometry and ¹H NMR spectroscopy and mononuclear complex species were determined; [In(Pic)]²⁺ (log<em>β</em>_<em>011</em> = 6.94(4)), [In(Pic)₂]⁺ (log<em>β</em>_<em>021</em> = 11.98(9)), [In(Dpic)]⁺ (log<em>β</em>_<em>011</em> = 10.42(6)), [In(Dpic)₂]⁻ (log<em>β</em>_<em>021</em> = 17.58(7)) and [In(Dpic)₂(OH)]²⁻ (log<em>β</em>_<em>−</em>_<em>121</em> = 10.18(6)). To confirm the complexes stability in 1 % DMSO, ¹H NMR spectra were measured (immediately after dissolution up to 96 h). Antimicrobial and anticancer assays indicate a more significant sensitivity of <em>S. aureus</em> bacteria and MDA-MB-231 cancer cells to the InPic complex (IC₅₀ = 25 and 340.7 μM) than to the InDpic (IC₅₀ = 50 and 975.4 μM). The interaction and binding mechanism of picolinic/dipicolinic acid and their indium(III) complexes with HSA (human serum albumin) were studied using fluorescence and CD spectroscopy. The results confirmed that the studied compounds had bound successfully to HSA, and the binding parameters and constants (<em>K</em>_<em>SV</em>, <em>K</em>_<em>q</em>, <em>K</em>_<em>b</em>) were calculated together with the number of binding sites. The binding forces were identified based on calculated thermodynamic parameters (<em>ΔG, ΔH, ΔS</em>). Synchronous spectra were used to study the microenvironment of Tyr and Trp residues and displacement assays revealed that site I was the preferred binding site. After binding, conformational changes were found to have occurred in the HSA molecule and the % α-helical content had decreased.</p></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112738"},"PeriodicalIF":3.8,"publicationDate":"2024-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142243100","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In the search for new gold metalloantibiotics: In vitro evaluation of Au(III) (C^S)-cyclometallated complexes","authors":"Paula Pérez-Ramos ,&nbsp;Yaiza Gabasa ,&nbsp;Enmanuel Cornielle ,&nbsp;Humberto Rodríguez-Solla ,&nbsp;Sara M. Soto ,&nbsp;Raquel G. Soengas","doi":"10.1016/j.jinorgbio.2024.112735","DOIUrl":"10.1016/j.jinorgbio.2024.112735","url":null,"abstract":"<div><p>A series of (C^S)-cyclometallated Au(III) cationic complexes of general formula [Au(dppta)(dtc)]⁺, [Au(dppta)(azmtd)]⁺ and [Au(dppta)(azc)Cl]⁺ (dppta = N,N-diisopropyl-<em>P</em>,<em>P</em>-diphenylphosphinothioic amide-κ²C,S; dtc = dithiocarbamate-κ²S,S′; azc = azolium-2-dithiocarboxylate-κ¹S; azmdt = azol(<em>in</em>)ium-2-(methoxy)methanedithiol-κ²S,S′) were synthetized and tested against a panel of bacterial strains belonging to different Gram-positive and Gram-negative species of the ESKAPE group of pathogens. Among the tested compounds, complex <strong>4c</strong> had the higher Therapeutic Index (TI) against multidrug resistant strains of <em>S. aureus</em>, <em>S. epidermidis</em> and <em>A. baumannii</em>, showing a more favourable cytotoxicity profile than the reference gold metalloantibiotic Auranofin.</p><p>© 2024 xxxxxxxx. Hosting by Elsevier B.V. All rights reserved.</p></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112735"},"PeriodicalIF":3.8,"publicationDate":"2024-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0162013424002599/pdfft?md5=6a2820dc9d1d49c64fbf07f7777892bd&pid=1-s2.0-S0162013424002599-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142232130","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural and functional mechanisms of cytochrome c oxidase","authors":"Denis L. Rousseau,&nbsp;Izumi Ishigami,&nbsp;Syun-Ru Yeh","doi":"10.1016/j.jinorgbio.2024.112730","DOIUrl":"10.1016/j.jinorgbio.2024.112730","url":null,"abstract":"<div><p>Cytochrome <em>c</em> oxidase (C<em>c</em>O) is the terminal enzyme in the electron transfer chain in mitochondria. It catalyzes the four-electron reduction of O₂ to H₂O and harnesses the redox energy to drive unidirectional proton translocation against a proton electrochemical gradient. A great deal of research has been conducted to comprehend the molecular properties of C<em>c</em>O. However, the mechanism by which the oxygen reduction reaction is coupled to proton translocation remains poorly understood. Here, we review the chemical properties of a variety of key oxygen intermediates of bovine C<em>c</em>O (bC<em>c</em>O) revealed by time-resolved resonance Raman spectroscopy and the structural features of the enzyme uncovered by serial femtosecond crystallography, an innovative technique that allows structural determination at room temperature without radiation damage. The implications of these data on the proton translocation mechanism are discussed.</p></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112730"},"PeriodicalIF":3.8,"publicationDate":"2024-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142173831","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}