Katharina Trost , Robert B. Gennis , John F. Allen , Daniel B. Mills , William F. Martin
{"title":"Oxygen reductase origin followed the great oxidation event and terminated the Lomagundi excursion","authors":"Katharina Trost , Robert B. Gennis , John F. Allen , Daniel B. Mills , William F. Martin","doi":"10.1016/j.bbabio.2025.149575","DOIUrl":"10.1016/j.bbabio.2025.149575","url":null,"abstract":"<div><div>The history of Earth's atmospheric oxygen is a cornerstone of evolutionary biology. While unequivocal evidence for an increase in atmospheric O<sub>2</sub> marks the Great Oxidation Event (GOE) roughly 2.4 billion years ago, evidence underlying proposals for pre-GOE O<sub>2</sub> accumulation is debated. Here we have investigated the distribution of genes for oxygen reductases, the enzymes that consume O<sub>2</sub> in respiratory chains, across independently generated molecular timescales of prokaryotic evolution. The data indicate that cytochrome <em>bd</em>-oxidases, heme-copper oxidases and alternative oxidases arose in the wake of the GOE ca. 2.4 billion years ago, after which the genes were subjected to abundant lateral gene transfer, a reflection of their utility in redox balance and membrane bioenergetics. The data lead us to propose a straightforward four-stage model for O<sub>2</sub> accumulation surrounding the GOE: (i) Negligible O<sub>2</sub> existed prior to the GOE. (ii) Cyanobacterial O<sub>2</sub> production started at the GOE, yet was capped at 2 % [<em>v</em>/v] atmospheric O<sub>2</sub>, the threshold at which cyanobacterial nitrogenase is inhibited by O<sub>2</sub>. (iii) Production of 0.02 atm of O<sub>2</sub> (2 % [<em>v</em>/v]) at the GOE buried roughly the entire atmospheric CO<sub>2</sub> inventory, causing sudden enrichment of <sup>13</sup>C in dissolved inorganic carbon (the Lomagundi <sup>13</sup>C anomaly), through RuBisCO isotope discrimination, without atmospheric O<sub>2</sub> exceeding 2 % [<em>v</em>/v]. (iv) High atmospheric <sup>12</sup>C at the end of the Lomagundi excursion marks the origin of oxygen reductases, their rapid spread via function in respiratory CO<sub>2</sub> liberation, and the onset of equilibrium between photosynthetic O<sub>2</sub> production and respiratory O<sub>2</sub> consumption at 2 % atmospheric O<sub>2</sub>.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149575"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145670512","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}
Cleo Bagchus , Lennart A.I. Ramakers , Dana Verhoeven , Claudia Beraldo , Alessandro Alboresi , Tomas Morosinotto , Herbert van Amerongen , Emilie Wientjes
{"title":"Quantitative decomposition of non-photochemical quenching in Physcomitrium patens highlights synergistic roles of LhcSR and zeaxanthin","authors":"Cleo Bagchus , Lennart A.I. Ramakers , Dana Verhoeven , Claudia Beraldo , Alessandro Alboresi , Tomas Morosinotto , Herbert van Amerongen , Emilie Wientjes","doi":"10.1016/j.bbabio.2026.149581","DOIUrl":"10.1016/j.bbabio.2026.149581","url":null,"abstract":"<div><div>Non-photochemical quenching (NPQ) is a collective term for photoprotective processes that safely dissipate excess light energy as heat. The moss <em>Physcomitrium patens</em> is an interesting species for the study of NPQ as it contains PsbS (indispensable for NPQ in vascular plants), LhcSR (indispensable for NPQ in green algae) and a xanthophyll cycle, which interconverts violaxanthin (Vx) and zeaxanthin (Zx) and is also imperative for NPQ. Here, we aimed to disentangle the individual contributions of PsbS, LhcSR and Zx to NPQ. NPQ induction and relaxation were measured for wild-type <em>P. patens</em> and thirteen mutants with altered NPQ at a wide range of light intensities. We applied a multivariate data analysis pipeline to find distinct kinetic components underlying NPQ, together with their contributions to NPQ. A slowly-rising component provides most NPQ, especially at higher light intensities. Another component contains a transient NPQ peak with a fast rise, providing quick protection, and requires the presence of either PsbS or LhcSR. Both components are enhanced by the combined presence of Zx and LhcSR. While PsbS-related NPQ is less dependent on Zx, in contrast to the situation in vascular plants, Vx to Zx conversion enhances LhcSR-related NPQ at all light intensities and within the first minute of illumination. The influence of Zx is thus broader than previously recognized, especially through its synergistic interaction with LhcSR.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149581"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145994645","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":"Recover a long-missing thermodynamic limit from experimental trajectories of F1-ATPase molecular motor","authors":"Ruizheng Hou , Shoichi Toyabe , Zhisong Wang","doi":"10.1016/j.bbabio.2026.149583","DOIUrl":"10.1016/j.bbabio.2026.149583","url":null,"abstract":"<div><div>In the field of molecular motors, a general thermodynamic limit is widely used in theories but long missing in experiments. By this limit, a motor's forward-to-backward stepping ratio obeys a distinct full-step scaling with an opposing force, and is further related to a thermodynamic force that may inform the motor's stall force and energy efficiency from low-force experiments or even force-independent optical tracking experiments. This limit is now recovered directly from experimental trajectories of F<sub>1</sub>-ATPase motor – in a strict ‘double-blind’ test with the thermodynamic force and the stepping ratio extracted independently from the trajectories by an improved statistical method and a rigorous thermodynamic analysis based on Jarzynski equality. This study thus removes a long-standing controversy in the field of molecular motors, and significantly reduces the difficulty of stall force measurement. Notably, this study also enables experimental access to the elusive stepping ratio, which is essentially a ratio of cycle fluxes and hence difficult to measure so far. Finally, the Jarzynski equality-based thermodynamic analysis is comprehensive, providing a unified conceptual framework to analyze evolutionary optimality of biological molecular motors and guide development of artificial molecular motors.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149583"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146022658","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}
Lu Wang , Yi-Hao Yan , Guang-Lei Wang , Xing-Yu Yue , Chen-Hui Qi , Mei-Juan Zou , Zheng-Yu Wang-Otomo , Michael T. Madigan , Yueyong Xin , Long-Jiang Yu
{"title":"Assembly, selectivity, and compatibility of bacterial photosynthetic complexes from divergent species detected in a chimeric strain","authors":"Lu Wang , Yi-Hao Yan , Guang-Lei Wang , Xing-Yu Yue , Chen-Hui Qi , Mei-Juan Zou , Zheng-Yu Wang-Otomo , Michael T. Madigan , Yueyong Xin , Long-Jiang Yu","doi":"10.1016/j.bbabio.2026.149584","DOIUrl":"10.1016/j.bbabio.2026.149584","url":null,"abstract":"<div><div>Photosynthetic complexes comprising light-harvesting (LH) and reaction center (RC) components are essential for biological energy conversion in photosynthesis. Assembly of these multi-protein structures is a topic of great interest, and assembly mechanisms appear to reflect the evolutionary diversity of the particular phototrophic organism. Here we constructed a photosynthetic chimera expressing the <em>Roseiflexus castenholzii</em> LH and <em>Rhodospirillum rubrum</em> RC complexes in a photocomplex–deficient <em>Rsp. rubrum</em> mutant, and spectroscopy confirmed LH expression with absorption maxima at 878 and 801 nm. The chimeric strain grew slower phototrophically than wildtype but faster than a strain containing only the RC, indicating partial energy transfer from LH to RC. Cryo-EM structural analysis revealed that the <em>Rfl</em>. <em>castenholzii</em> LH independently assembled into a closed ring of 15 αβ heterodimers lacking carotenoids, resulting in a blue-shifted Q<sub>y</sub> transition, while the <em>Rsp</em>. <em>rubrum</em> RC formed a separate complex with an RC:LH ratio of ∼17:1 instead of a typical 1:1. Structural differences, including the absence of two <em>Rfl</em>. <em>castenholzii</em>-specific small proteins, likely precluded formation of a conjoined LH–RC in the chimeric strain. These results reveal that distinct photocomplex assembly strategies exist in phylogenetically divergent species and underscore the modularity and adaptability of photosynthetic complexes, offering insights for artificial photosystem design.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149584"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146087973","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":"A red-shifted LHCII in Chlamydomonas priscui allows for efficient light harvesting under an Antarctic lake","authors":"Sam Wilson , Jun Minagawa","doi":"10.1016/j.bbabio.2025.149579","DOIUrl":"10.1016/j.bbabio.2025.149579","url":null,"abstract":"<div><div>The psychrophilic green alga <em>Chlamydomonas priscui</em> was isolated from an Antarctic lake, where it has adapted to low light, low temperature, and high salinity environment. How photosynthetic light harvesting adjusts to such conditions remains an important question. Here, we present biochemical, biophysical, and phylogenetic analyses of the major light-harvesting complex II (LHCII) of <em>C. priscui</em> (CpLHCII). Compared to the LHCII of the mesophilic model alga <em>C. reinhardtii</em> (CrLHCII), CpLHCII has a chlorophyll (Chl) <em>a</em>:<em>b</em> ratio of ~1 (CrLHCII Chl <em>a</em>:<em>b</em> = ~1.24), with an intermediate red Chl <em>a</em> species replaced by Chl <em>b</em> and altered spectral tuning of Chl <em>a</em>. These changes cause an overall red shift in absorption, apparently driven by specific mutations in the primary sequence of CpLHCII. Consequently, CpLHCII shows enhanced energy transfer efficiency, in particular for energy harvested in the blue-green region directed to Chl <em>a</em>. These characteristics indicate a light-harvesting system with reduced energy loss, with respect to CrLHCII. We propose that the unique properties of CpLHCII aids survival in the extreme, spectrally-limited light conditions posed by <em>C. priscui</em>'s ecological niche and suggest that these features could inform strategies to optimize light harvesting in agriculture and biotechnology.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149579"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145834593","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":"Electrical acceleration of the glycerophosphate shuttle by the VDAC1,2-hexokinase complexes of mitochondria","authors":"Victor V. Lemeshko","doi":"10.1016/j.bbabio.2026.149586","DOIUrl":"10.1016/j.bbabio.2026.149586","url":null,"abstract":"<div><div>Glycerophosphate shuttle, an important crossroad between oxidative phosphorylation system, glycolysis and lipid metabolism, consists of the rate-limiting mitochondrial glycerol-3-phosphate dehydrogenase (GPD2) and the cytosolic dehydrogenase (GPD1). GPD2 level is relatively high in islet beta-cells, spermatozoa and neurons, required abruptly rapid periodic ATP consumption, as well as in rapidly growing normal tissues during neonatal period and many cancers. According to the computational model developed in the present work, the glycerophosphate shuttle should be significantly activated by the outer membrane potential (OMP) generated by the VDAC1,2-hexokinase complexes of mitochondrial outer membrane. This is due to the capture of cytosolic glycerol-3-phosphate<sup>2−</sup> into the mitochondrial intermembrane space by the positive OMP, thus increasing its local concentration near GPD2. The predicted acceleration is most significant at relatively high <em>K</em><sub>m</sub> of GPD2 for glycerol-3-phosphate<sup>2−</sup> and strongly modulated by the VDAC's voltage-gating properties. In general, OMP generated by the VDAC1,2-hexokinase complexes might play a crucial role in the above-mentioned crossroad, converting it into the “electrical metabolic crossroad”. The suggested electrical deviation of glycolysis towards the mitochondrial GPD2, as a tool for the metabolic shift to an accelerated aerobic glycolysis without an inhibition of mitochondrial respiration, highlights this metabolic switching as one of the possible options of the Warburg effect.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149586"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147319050","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}
Kilian Zuchan , Nina Breuer , Christoph Laurich , Wolfgang Nitschke , Frauke Baymann , James A. Birrell
{"title":"Thermodynamic landscape of the redox-centres in the electron-confurcating [FeFe]-Hydrogenase (TmHydABC) of Thermotoga maritima","authors":"Kilian Zuchan , Nina Breuer , Christoph Laurich , Wolfgang Nitschke , Frauke Baymann , James A. Birrell","doi":"10.1016/j.bbabio.2025.149577","DOIUrl":"10.1016/j.bbabio.2025.149577","url":null,"abstract":"<div><div>The heterotrimeric [FeFe]‑hydrogenase (<em>Tm</em>HydABC) from <em>Thermotoga maritima</em> synergistically uses electrons from ferredoxin and NADH to reduce protons to hydrogen enabling the anaerobic metabolism of carbohydrates and other molecules. The precise mechanism by which this flavin-based electron confurcation is achieved is still unknown. Here, the redox properties of the cofactors in <em>Tm</em>HydABC were characterized via chemical and electrochemical redox titrations monitored by EPR- and UV/Vis-spectroscopy. Deconvolution of nine out of eleven iron‑sulfur clusters harboured by the apo-enzyme was achieved by (a) exploiting the distinct relaxation properties (and hence temperature-dependencies) of the EPR-signals, (b) making use of spectral idiosyncrasies of [4Fe-4S] versus thioredoxin-like [2Fe-2S] clusters in UV/Vis-spectroscopy and (c) using the individual HydA, HydB and HydC subunits and C-terminal domains of HydA and HydB. Furthermore, electrostatic interactions between certain neighbouring clusters and a paramagnetic interaction between the flavin and one of the iron‑sulfur clusters were revealed. The electrochemical parameters of the flavin were obtained both via UV/Vis-spectroscopy and EPR-analysis of its semi-reduced state in isolated HydB. This semi-reduced state was found to correspond to a neutral flavosemiquinone and a pK<sub>a</sub> (attributed to the N5-proton) was extracted from the pH-dependence of its redox midpoint potential. The electrochemical properties of the flavin in the entire enzyme appear to differ significantly from those in the isolated HydB subunit. The flavin and iron‑sulfur cluster redox properties indicate a dynamic electrochemical landscape, potentially contributing to its mechanism.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149577"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145806242","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":"Utilization of minor red-shifted chlorophyll a for oxygenic photosynthesis under far-red light in green algae","authors":"Fei Wang , Seiji Akimoto , Masami Kobayashi , Hideaki Miyashita","doi":"10.1016/j.bbabio.2026.149582","DOIUrl":"10.1016/j.bbabio.2026.149582","url":null,"abstract":"<div><div>Several eukaryotic alga species can perform oxygenic photosynthesis under far-red (FR) light using light-harvesting complexes that absorb this light. We previously isolated a green alga, <em>Neochloris</em> sp. Biwa 5-2, which can grow under FR LED light. However, the mechanisms that support photosynthesis and enable growth under such conditions remain unclear. Here, we performed spectroscopic analyses to investigate light harvesting and excitation-energy transfer in <em>Neochloris</em> sp. Biwa 5-2 under FR light. Two types of minor red-shifted chlorophyll <em>a</em> (Chl <em>a</em>), Chl 706 and Chl 718, were identified as pigments that can absorb light and contribute to oxygenic photosynthesis under FR conditions. Time-resolved fluorescence spectroscopy confirmed that these pigments were involved in excitation-energy transfer via an uphill energy transfer process. During this process, <em>Neochloris</em> sp. Biwa 5-2 uses constitutively present minor red-shifted Chl <em>a</em> to harvest FR light and sustain photosynthesis. This study appears to be the first report of minor Chl <em>a</em> functioning as a primary light-harvesting pigment that enables growth under FR light.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149582"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146004659","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}
Makhmadyusuf Khasimov , Ekaterina P. Petushkova , Ekaterina V. Mayorova , Ilya V. Timofeev , Natalia N. Rudenko , Anatoly A. Tsygankov
{"title":"HydSL hydrogenase of Thiocapsa bogorovii may participate in sulfur respiration","authors":"Makhmadyusuf Khasimov , Ekaterina P. Petushkova , Ekaterina V. Mayorova , Ilya V. Timofeev , Natalia N. Rudenko , Anatoly A. Tsygankov","doi":"10.1016/j.bbabio.2026.149585","DOIUrl":"10.1016/j.bbabio.2026.149585","url":null,"abstract":"<div><div>According to the modern classification of NiFe hydrogenases, the HydSL hydrogenase of <em>Thiocapsa bogorovii</em> is assigned to subgroup 1e, the so-called isp-type hydrogenases. This subgroup is proposed to unite hydrogenases involved in sulfur respiration; however, direct experimental evidence supporting this function remains limited. In this study, we isolated a protein complex containing the HydSL hydrogenase from <em>T. bogorovii</em> that exhibits high activity in the H₂ + S<sup>0</sup> → H₂S reaction. Under native electrophoresis, the complex migrated as a single band, whereas SDS-PAGE resolved it into seven bands, four of which matched the molecular masses of HydS, Isp1, Isp2, and HydL proteins.</div><div>Incubation of <em>T. bogorovii</em> cells in a hydrogen atmosphere in darkness and in the presence of elemental sulfur resulted in increased expression of the <em>hydS</em>, <em>hydL</em>, <em>isp1</em>, and <em>isp2</em> genes encoding the subunits and partner proteins of the complex. The elevated transcript levels correlated with increased cellular activity in the reduction of elemental sulfur to hydrogen sulfide. These observations indicate that the HydSL-containing protein complex may participate in sulfur respiration in <em>T. bogorovii</em> under dark, anaerobic conditions in the absence of oxygen and fermentable substrates. Based on these results and literature data, we propose a putative mechanism for the complex, consistent with its designation as a sulfhydrogenase.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149585"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147272751","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":"Demand-only energetics at 120 ATP per glucose: A reply to Lynch","authors":"William F. Martin","doi":"10.1016/j.bbabio.2026.149587","DOIUrl":"10.1016/j.bbabio.2026.149587","url":null,"abstract":"<div><div>Recently in these pages, a paper by Lynch appeared in response to a report showing that his numbers for biosynthetic costs (ATP demand) in cells are inflated, so much so that they would require <em>E. coli</em> to obtain >100 ATP per glucose and mitochondria to obtain >240 ATP per glucose. The inflated estimates trace to one factor: Lynch exclusively considers ATP demand and systematically neglects ATP supply—the essence of bioenergetics. Thermodynamics stipulate that a cell cannot grow if its ATP demands exceed its ATP supply. Here I compare Lynch's calculated ATP demands to laboratory measurements of the ATP supply that <em>E. coli</em> synthesizes during cell division. The results bear out my case, and leave no doubt: Lynch's calculations require <em>E. coli</em> to synthesize ∼120 ATP per glucose, which is thermodynamically impossible. As a consequence, his demand-only ‘energetic’ attacks on mitochondria and endosymbiosis in evolution are baseless.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149587"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147373521","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}