Dynamic modulation of transthylakoid electric potential by chloroplast ATP synthases

IF 3.3 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Hui Lyu, Yong-Song Zuo
{"title":"Dynamic modulation of transthylakoid electric potential by chloroplast ATP synthases","authors":"Hui Lyu,&nbsp;Yong-Song Zuo","doi":"10.1016/j.biochi.2024.01.007","DOIUrl":null,"url":null,"abstract":"<div><p>The light-induced transthylakoid membrane potential (ΔΨ<sub>m</sub>) can function as a driving force to help catalyzing the formation of ATP molecules, proving a tight connection between ΔΨ<sub>m</sub><span> and the ATP synthase. Naturally, a question can be raised on the effects of altered functioning of ATP synthases on regulating ΔΨ</span><sub>m</sub>, which is attractive in the area of photosynthetic research. Lots of findings, when making efforts of solving this difficulty, can offer an in-depth understanding into the mechanism behind. However, the functional network on modulating ΔΨ<sub>m</sub> is highly interdependent. It is difficult to comprehend the consequences of altered activity of ATP synthases on adjusting ΔΨ<sub>m</sub> because parameters that have influences on ΔΨ<sub>m</sub> would themselves be affected by ΔΨ<sub>m</sub><span>. In this work, a computer model was applied to check the kinetic changes in polarization/depolarization across the thylakoid membrane<span> (TM) regulated by the modified action of ATP synthases. The computing data revealed that under the extreme condition by numerically “switching off” the action of the ATP synthase, the complete inactivation of ATP synthase would markedly impede proton translocation at the cytb</span></span><sub>6</sub>f complex. Concurrently, the KEA3 (CLCe) porter, actively pumping protons into the stroma, further contributes to achieving a sustained low level of ΔΨ<sub>m</sub>. Besides, the quantitative consequences on every particular component of ΔΨ<sub>m</sub> adjusted by the modified functioning of ATP synthases were also explored. By employing the model, we bring evidence from the theoretical perspective that the ATP synthase is a key factor in forming a transmembrane proton loop thereby maintaining a propriate steady-state ΔΨ<sub>m</sub> to meet variable environmental conditions.</p></div>","PeriodicalId":251,"journal":{"name":"Biochimie","volume":"221 ","pages":"Pages 27-37"},"PeriodicalIF":3.3000,"publicationDate":"2024-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimie","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0300908424000257","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

The light-induced transthylakoid membrane potential (ΔΨm) can function as a driving force to help catalyzing the formation of ATP molecules, proving a tight connection between ΔΨm and the ATP synthase. Naturally, a question can be raised on the effects of altered functioning of ATP synthases on regulating ΔΨm, which is attractive in the area of photosynthetic research. Lots of findings, when making efforts of solving this difficulty, can offer an in-depth understanding into the mechanism behind. However, the functional network on modulating ΔΨm is highly interdependent. It is difficult to comprehend the consequences of altered activity of ATP synthases on adjusting ΔΨm because parameters that have influences on ΔΨm would themselves be affected by ΔΨm. In this work, a computer model was applied to check the kinetic changes in polarization/depolarization across the thylakoid membrane (TM) regulated by the modified action of ATP synthases. The computing data revealed that under the extreme condition by numerically “switching off” the action of the ATP synthase, the complete inactivation of ATP synthase would markedly impede proton translocation at the cytb6f complex. Concurrently, the KEA3 (CLCe) porter, actively pumping protons into the stroma, further contributes to achieving a sustained low level of ΔΨm. Besides, the quantitative consequences on every particular component of ΔΨm adjusted by the modified functioning of ATP synthases were also explored. By employing the model, we bring evidence from the theoretical perspective that the ATP synthase is a key factor in forming a transmembrane proton loop thereby maintaining a propriate steady-state ΔΨm to meet variable environmental conditions.

叶绿体 ATP 合成酶对跨叶绿体电动势的动态调节
光诱导的跨类囊体膜电位(ΔΨm)可作为一种驱动力,帮助催化 ATP 分子的形成,这证明了ΔΨm 与 ATP 合成酶之间的紧密联系。自然而然,人们会提出 ATP 合成酶功能改变对调节ΔΨm 的影响问题,这在光合作用研究领域很有吸引力。在努力解决这一难题的过程中,许多研究成果都能让人深入了解其背后的机制。然而,调节ΔΨm 的功能网络是高度相互依存的。由于对ΔΨm有影响的参数本身也会受到ΔΨm的影响,因此很难理解ATP合成酶活性的改变对调节ΔΨm的影响。在这项工作中,应用计算机模型检验了在 ATP 合成酶作用改变的调节下,整个类囊体膜(TM)极化/去极化的动力学变化。计算数据显示,在数值 "关闭 "ATP合成酶作用的极端条件下,ATP合成酶的完全失活将明显阻碍质子在细胞b6f复合物上的转运。与此同时,KEA3(CLCe)搬运工积极地将质子泵入基质,进一步促进了ΔΨm水平的持续降低。此外,我们还探讨了 ATP 合成酶的功能改变对ΔΨm 各特定成分的定量影响。通过运用该模型,我们从理论上证明了ATP合成酶是形成跨膜质子环从而维持适当稳态ΔΨm以适应多变环境条件的关键因素。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Biochimie
Biochimie 生物-生化与分子生物学
CiteScore
7.20
自引率
2.60%
发文量
219
审稿时长
40 days
期刊介绍: Biochimie publishes original research articles, short communications, review articles, graphical reviews, mini-reviews, and hypotheses in the broad areas of biology, including biochemistry, enzymology, molecular and cell biology, metabolic regulation, genetics, immunology, microbiology, structural biology, genomics, proteomics, and molecular mechanisms of disease. Biochimie publishes exclusively in English. Articles are subject to peer review, and must satisfy the requirements of originality, high scientific integrity and general interest to a broad range of readers. Submissions that are judged to be of sound scientific and technical quality but do not fully satisfy the requirements for publication in Biochimie may benefit from a transfer service to a more suitable journal within the same subject area.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信