Biochimica et Biophysica Acta-Bioenergetics最新文献

{"title":"Applied photosynthesis: An idea whose time has come","authors":"Barry D. Bruce ,&nbsp;Suleyman I. Allakhverdiev","doi":"10.1016/j.bbabio.2024.149525","DOIUrl":"10.1016/j.bbabio.2024.149525","url":null,"abstract":"<div><div>Advancements in materials science, synthetic biology, and nanomaterial engineering are revolutionizing renewable energy technologies, creating new pathways for sustainable energy production. Biohybrid devices—systems combining biological components with engineered synthetic materials—are emerging as powerful platforms for harnessing solar energy to drive hydrogen production, photovoltaics, catalysis, and biosensing. This collection of articles presents leading-edge research in biohybrid energy systems, where photosynthetic mechanisms are redeployed to develop eco-friendly, high-efficiency alternatives to conventional solar technologies. Central to these biohybrid designs are diverse organisms, from cyanobacteria and algae to purple bacteria and archaea, enabling researchers to employ a broad range of bioengineered proteins and photosynthetic complexes. By integrating advances in synthetic biology with precision nanomaterial fabrication, scientists can improve protein functionality and device stability at the nanoscale, optimizing these systems for light absorption, energy conversion, and resilience. This convergence allows exploring unique photoactive pigments, including type I and type II reaction centers, specialized light-harvesting and retinal-binding proteins. Through protein engineering and careful selection of photoactive components, biohybrid devices offer promising solutions for sustainable energy applications, positioning photosynthetic organisms as critical contributors to innovative energy technology.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 1","pages":"Article 149525"},"PeriodicalIF":3.4,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142689557","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"WITHDRAWN: There is often - But not always - An alternative!","authors":"Howard T Jacobs, Anthony L Moore","doi":"10.1016/j.bbabio.2024.149534","DOIUrl":"10.1016/j.bbabio.2024.149534","url":null,"abstract":"<p><p>The Publisher regrets that this article is an accidental duplication of an article that has already been published, https://doi.org/10.1016/j.bbabio.2024.149534. The duplicate article has therefore been withdrawn. The full Elsevier Policy on Article Withdrawal can be found at https://www.elsevier.com/about/policies/article-withdrawal.</p>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":" ","pages":"149534"},"PeriodicalIF":3.4,"publicationDate":"2024-12-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142886409","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"There is often – but not always – an alternative!","authors":"Howard T. Jacobs ,&nbsp;Anthony L. Moore","doi":"10.1016/j.bbabio.2024.149533","DOIUrl":"10.1016/j.bbabio.2024.149533","url":null,"abstract":"","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149533"},"PeriodicalIF":3.4,"publicationDate":"2024-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142878512","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An analysis of the structural changes of the oxygen evolving complex of Photosystem II in the S1 and S3 states revealed by serial femtosecond crystallography","authors":"Salma Yehia ,&nbsp;Jimin Wang ,&nbsp;Gary W. Brudvig ,&nbsp;M.R. Gunner ,&nbsp;Bernard R. Brooks ,&nbsp;Muhamed Amin","doi":"10.1016/j.bbabio.2024.149531","DOIUrl":"10.1016/j.bbabio.2024.149531","url":null,"abstract":"<div><div>Photosystem II (PSII) is a unique natural catalyst that converts solar energy into chemical energy using earth abundant elements in water at physiological pH. Understanding the reaction mechanism will aid the design of biomimetic artificial catalysts for efficient solar energy conversion. The Mn₄O₅Ca cluster cycles through five increasingly oxidized intermediates before oxidizing two water molecules into O₂ and releasing protons to the lumen and electrons to drive PSII reactions. The Mn coordination and OEC electronic structure changes through these intermediates. Thus, obtaining a high-resolution structure of each catalytic intermediate would help reveal the reaction mechanism. While valuable structural information was obtained from conventional X-ray crystallography, time-resolution of conventional X-ray crystallography limits the analysis of shorted-lived reaction intermediates. Serial Femtosecond X-ray crystallography (SFX), which overcomes the radiation damage by using ultra short laser pulse for imaging, has been used extensively to study the water splitting intermediates in PSII. Here, we review the state of the art and our understanding of the water splitting reaction before and after the advent of SFX. Furthermore, we analyze the likely Mn coordination in multiple XFEL structures prepared in the dark-adapted S₁ state and those following two-flashes which are poised in the penultimate S₃ oxidation state based on Mn coordination chemistry. Finally, we summarize the major contributions of the SFX to our understanding of the structures of the S₁ and S₃ states.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149531"},"PeriodicalIF":3.4,"publicationDate":"2024-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142856529","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Acute treadmill exercise induces mitochondrial unfolded protein response in skeletal muscle of male rats","authors":"Ibrahim Turkel ,&nbsp;Gokhan Burcin Kubat ,&nbsp;Tugba Fatsa ,&nbsp;Ozgu Acet ,&nbsp;Berkay Ozerklig ,&nbsp;Burak Yazgan ,&nbsp;Gulcin Simsek ,&nbsp;Keshav K. Singh ,&nbsp;Sukran Nazan Kosar","doi":"10.1016/j.bbabio.2024.149532","DOIUrl":"10.1016/j.bbabio.2024.149532","url":null,"abstract":"<div><div>Mitochondria are often referred to as the energy centers of the cell and are recognized as key players in signal transduction, sensing, and responding to internal and external stimuli. Under stress conditions, the mitochondrial unfolded protein response (UPR^mt), a conserved mitochondrial quality control mechanism, is activated to maintain mitochondrial and cellular homeostasis. As a physiological stimulus, exercise-induced mitochondrial perturbations trigger UPR^mt, coordinating mitochondria-to-nucleus communication and initiating a transcriptional program to restore mitochondrial function. The aim of this study was to evaluate the UPR^mt signaling response to acute exercise in skeletal muscle. Male rats were subjected to acute treadmill exercise at 25 m/min for 60 min on a 0 % grade. Plantaris muscles were collected from both sedentary and exercise groups at various times: immediately (0), and at 1, 3, 6, 12, and 24 h post-exercise. Reactive oxygen species (ROS) production was assessed using hydrogen peroxide assay and dihydroethidium staining. Additionally, the mRNA and protein expression of UPR^mt markers were measured using ELISA and real-time PCR. Mitochondrial activity was assessed using succinate dehydrogenase (SDH) and cytochrome <em>c</em> oxidase (COX) staining. Our results demonstrated that acute exercise increased ROS production and upregulated UPR^mt markers at both gene and protein levels. Moreover, skeletal muscle exhibited an increase in mitochondrial activity in response to exercise, as indicated by SDH and COX staining. These findings suggest that acute treadmill exercise is sufficient to induce ROS production, activate UPR^mt signaling, and enhance mitochondrial activity in skeletal muscle, expanding our understanding of mitochondrial adaptations to exercise.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149532"},"PeriodicalIF":3.4,"publicationDate":"2024-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142830704","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Species differences in glycerol-3-phosphate metabolism reveals trade-offs between metabolic adaptations and cell proliferation","authors":"Kateryna Gaertner ,&nbsp;Mügen Terzioglu ,&nbsp;Craig Michell ,&nbsp;Riikka Tapanainen ,&nbsp;Jaakko Pohjoismäki ,&nbsp;Eric Dufour ,&nbsp;Sina Saari","doi":"10.1016/j.bbabio.2024.149530","DOIUrl":"10.1016/j.bbabio.2024.149530","url":null,"abstract":"<div><div>The temperate climate-adapted brown hare (<em>Lepus europaeus</em>) and the cold-adapted mountain hare (<em>Lepus timidus</em>) are closely related and interfertile species. However, their skin fibroblasts display distinct gene expression profiles related to fundamental cellular processes. This indicates important metabolic divergence between the two species. Through targeted metabolomics and metabolite tracing, we identified species-specific variations in glycerol 3-phosphate (G3P) metabolism. G3P is a key metabolite of the G3P shuttle, which transfers reducing equivalents from cytosolic NADH to the mitochondrial electron transport chain (ETC), consequently regulating glycolysis, lipid metabolism, and mitochondrial bioenergetics. Alterations in G3P metabolism have been implicated in multiple human pathologies including cancer and diabetes. We observed that mountain hare mitochondria exhibit elevated G3P shuttle activity, alongside increased membrane potential and decreased mitochondrial temperature. Silencing mitochondrial G3P dehydrogenase (GPD2), which couples the conversion of G3P to the ETC, uncovered its species-specific role in controlling mitochondrial membrane potential and highlighted its involvement in skin fibroblast thermogenesis. Unexpectedly, GPD2 silencing enhanced wound healing and cell proliferation rates in a species-specific manner. Our study underscores the pivotal role of the G3P shuttle in mediating physiological, bioenergetic, and metabolic divergence between these hare species.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149530"},"PeriodicalIF":3.4,"publicationDate":"2024-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142781483","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inside-out submitochondrial particles affect the mitochondrial permeability transition pore opening under conditions of mitochondrial dysfunction","authors":"Cristina Algieri ,&nbsp;Antonia Cugliari ,&nbsp;Patrycja Anna Glogowski ,&nbsp;Silvia Granata ,&nbsp;Micaela Fabbri ,&nbsp;Fabiana Trombetti ,&nbsp;Maria Laura Bacci ,&nbsp;Salvatore Nesci","doi":"10.1016/j.bbabio.2024.149528","DOIUrl":"10.1016/j.bbabio.2024.149528","url":null,"abstract":"<div><div>The inside-out submitochondrial particles (IO-SMPs) showed a strong protective effect against mitochondrial permeability transition pore (mPTP) opening in mitochondria isolated from swine hearts 3 h after explantation. The latter condition was used to emulate situation of mitochondrial damage. We identified that the protective effect of IO-SMPs cannot be attributed to a functional modulation of the enzymatic complexes involved in mPTP formation. Indeed, oxidative phosphorylation and F₁F_O-ATPase activity were not affected. Conversely, mPTP desensitization might be caused by structural modification. IO-SMP incorporation into the mitochondria can modulate the membrane-bound enzyme complexes' functionality, inducing F₁F_O-ATPase to be unable to carry out the conformational changes useful for mPTP opening. Thus, the data are a valid starting point for IO-SMP application in the treatment of impaired cardiovascular conditions supported by mPTP opening.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 1","pages":"Article 149528"},"PeriodicalIF":3.4,"publicationDate":"2024-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142757674","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alternative NADH dehydrogenase: A complex I backup, a drug target, and a tool for mitochondrial gene therapy","authors":"Dmytro V. Gospodaryov","doi":"10.1016/j.bbabio.2024.149529","DOIUrl":"10.1016/j.bbabio.2024.149529","url":null,"abstract":"<div><div>Alternative NADH dehydrogenase, also known as type II NADH dehydrogenase (NDH-2), catalyzes the same redox reaction as mitochondrial respiratory chain complex I. Specifically, it oxidizes reduced nicotinamide adenine dinucleotide (NADH) while simultaneously reducing ubiquinone to ubiquinol. However, unlike complex I, this enzyme is non-proton pumping, comprises of a single subunit, and is resistant to rotenone. Initially identified in bacteria, fungi and plants, NDH-2 was subsequently discovered in protists and certain animal taxa including sea squirts. The gene coding for NDH-2 is also present in the genomes of some annelids, tardigrades, and crustaceans. For over two decades, NDH-2 has been investigated as a potential substitute for defective complex I. In model organisms, NDH-2 has been shown to ameliorate a broad spectrum of conditions associated with complex I malfunction, including symptoms of Parkinson's disease. Recently, lifespan extension has been observed in animals expressing NDH-2 in a heterologous manner. A variety of mechanisms have been put forward by which NDH-2 may extend lifespan. Such mechanisms include the activation of pro-longevity pathways through modulation of the NAD⁺/NADH ratio, decreasing production of reactive oxygen species (ROS) in mitochondria, or then through moderate increases in ROS production followed by activation of defense pathways (mitohormesis). This review gives an overview of the latest research on NDH-2, including the structural peculiarities of NDH-2, its inhibitors, its role in the pathogenicity of mycobacteria and apicomplexan parasites, and its function in bacteria, fungi, and animals.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149529"},"PeriodicalIF":3.4,"publicationDate":"2024-11-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142774569","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ultrafast kinetics of PSI-LHCI super-complex from the moss Physcomitrella patens","authors":"Dongyang Liu ,&nbsp;Qiujing Yan ,&nbsp;Xiaochun Qin ,&nbsp;Lijin Tian","doi":"10.1016/j.bbabio.2024.149526","DOIUrl":"10.1016/j.bbabio.2024.149526","url":null,"abstract":"<div><div>Photosystem I (PSI) is a large membrane photosynthetic complex that harvests sunlight and drives photosynthetic electron transport. In both green algae and higher plants, PSI's ultrafast energy transfer and charge separation kinetics have been characterized. In contrast, it is not yet clear in <em>Physcomitrella patens</em>, even though moss is one of the earliest land plants and represents a critical stage in plant evolution. Here, we measured the time-resolved fluorescence of purified <em>Pp</em> PSI-LHCI at both room temperature (RT) and 77 K. Compared to the PSI kinetics of <em>Arabidopsis thaliana</em> at RT, we found that although the overall trapping time of <em>Pp</em> PSI-LHCI is nearly identical, ∼46 ps, their lifetimes at different wavelength regions differ. Specifically, <em>Pp</em> PSI-LHCI is slower in energy trapping below 720 nm but faster beyond. The slow-down of energy transfer between bulk chlorophylls (Chls, &lt;720 nm) in <em>Pp</em> PSI-LHCI is probably because of the larger spatial gap between the PSI core and LHCI belt, and the acceleration of trapping at longer wavelength is most likely due to the lack of low-energy red-shifted Chls (red Chls). Indeed, time-resolved fluorescence results at 77 K revealed only three types of red Chls of 702 nm, 712 nm, and 720 nm in <em>Pp</em> PSI-LHCI but failed to detect the red Chls of 735 nm that present in LHCI in higher plants. Finally, we briefly discussed the evolutionary adaptations of PSI-LHCI in the context of red Chls from green algae to mosses and to land plants.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 1","pages":"Article 149526"},"PeriodicalIF":3.4,"publicationDate":"2024-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142677553","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative thermo- and piezostability study of photosynthetic core complexes containing bacteriochlorophyll a or b","authors":"Margus Rätsep ,&nbsp;Liina Kangur ,&nbsp;Kristjan Leiger ,&nbsp;Zheng-Yu Wang-Otomo ,&nbsp;Arvi Freiberg","doi":"10.1016/j.bbabio.2024.149527","DOIUrl":"10.1016/j.bbabio.2024.149527","url":null,"abstract":"<div><div>The resilience of biological systems to fluctuating environmental conditions is a crucial evolutionary advantage. In this study, we examine the thermo- and piezo-stability of the LH1-RC pigment-protein complex, the simplest photosynthetic unit, in three species of phototropic purple bacteria, each containing only this core complex. Among these species, <em>Blastochloris viridis</em> and <em>Blastochloris tepida</em> utilize bacteriochlorophyll <em>b</em> as the main light-harvesting pigment, while <em>Rhodospirillum rubrum</em> relies on bacteriochlorophyll <em>a</em>. Through spectroscopic analyses, we observed limited reversibility in the effects of temperature and pressure, likely due to the malleability of pigment binding sites within the light-harvesting LH1 complex. In terms of thermal robustness, LH1 complexes in a detergent environment progressively dissociate into dimeric (B820) and monomeric (B777) subunits. However, in the native membrane, degradation primarily occurs directly into B777 without the intermediate formation of B820. Interestingly, while high-pressure compression of core complexes from <em>Blastochloris viridis</em> and <em>Blastochloris tepida</em> caused significant changes in compressibility around 1.3 kbar and the formation of B777 and B820 subunits upon decompression, no such compressibility changes or pressure-induced dissociation were observed in <em>Rhodospirillum rubrum</em> complexes, even at pressures as high as 11 kbar. This study reveals significant differences in the piezo- and thermal properties of phototrophs containing either BChl <em>a</em> or BChl <em>b</em>, underscoring the critical role of structural factors in understanding the temperature- and pressure-induced denaturation phenomena in photosynthetic complexes. <em>Rhodospirillum rubrum</em>, in particular, stands out as one of the most thermodynamically stable systems among phototrophic microorganisms, capable of withstanding temperatures up to 70 °C and pressures exceeding 11 kbar.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 1","pages":"Article 149527"},"PeriodicalIF":3.4,"publicationDate":"2024-11-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142669837","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}