Generation of reducing power in chemosynthesis IV. Energy-linked reduction of pyridine nucleotides by succinate in Thiobacillus novellus

M.I.H. Aleem
{"title":"Generation of reducing power in chemosynthesis IV. Energy-linked reduction of pyridine nucleotides by succinate in Thiobacillus novellus","authors":"M.I.H. Aleem","doi":"10.1016/0926-6593(66)90136-6","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The experiments described in this report have indicated that the reduction of NAD<sup>+</sup> by succinate in <em>Thiobacillus novellus</em> is energy-dependent. By blocking the electron transport chain with antimycin A, the endergonic reduction of NAD<sup>+</sup> by succinate required ATP. The pyridine nucleotide reduction involved the mediation of the flavoprotein system as Atabrine and Amytal inhibited the process.</p></span></li><li><span>2.</span><span><p>2. Added mammalian cytochrome <span><math><mtext>c</mtext></math></span> has been shown to couple with the electron transport chain of <em>T. novellus</em> thus effecting the catalysis of the generation of high-energy intermediates coupled to succinate oxidation in the absence of inorganic phosphate. The non-phosphorylated high-energy compounds thus can be generated either at coupling site II by oxidation of succinate with cytochrome <span><math><mtext>c</mtext></math></span> as electron acceptor under anaerobic conditions, or at sites II and III under aerobic conditions, or at site III by the oxidation of ferrocytochrome <span><math><mtext>c</mtext></math></span> involving electron transport to molecular oxygen through the cytochrome oxidase portion of the respiratory chain. In all cases the reduction of NAD<sup>+</sup> was driven by the generated high-energy intermediates involving reversal of electron transfer from the cytochrome <span><math><mtext>c</mtext></math></span> level.</p></span></li><li><span>3.</span><span><p>3. The energy-dependent reduction of NAD<sup>+</sup> by succinate involving reversal of electron transfer from the cytochrome <span><math><mtext>c</mtext></math></span> level was sensitive to 2,4-dinitrophenol, dicumarol and arsenate. It was also inhibited by atabrine and Amytal. Antimycin A was effective in partial inhibition of the reversal of electron transfer. In addition malonate and cyanide were found to be potent inhibitors. The mechanism for the generation and utilization of energy for the reversed electron flow, is discussed.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90136-6","citationCount":"22","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926659366901366","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 22

Abstract

  • 1.

    1. The experiments described in this report have indicated that the reduction of NAD+ by succinate in Thiobacillus novellus is energy-dependent. By blocking the electron transport chain with antimycin A, the endergonic reduction of NAD+ by succinate required ATP. The pyridine nucleotide reduction involved the mediation of the flavoprotein system as Atabrine and Amytal inhibited the process.

  • 2.

    2. Added mammalian cytochrome c has been shown to couple with the electron transport chain of T. novellus thus effecting the catalysis of the generation of high-energy intermediates coupled to succinate oxidation in the absence of inorganic phosphate. The non-phosphorylated high-energy compounds thus can be generated either at coupling site II by oxidation of succinate with cytochrome c as electron acceptor under anaerobic conditions, or at sites II and III under aerobic conditions, or at site III by the oxidation of ferrocytochrome c involving electron transport to molecular oxygen through the cytochrome oxidase portion of the respiratory chain. In all cases the reduction of NAD+ was driven by the generated high-energy intermediates involving reversal of electron transfer from the cytochrome c level.

  • 3.

    3. The energy-dependent reduction of NAD+ by succinate involving reversal of electron transfer from the cytochrome c level was sensitive to 2,4-dinitrophenol, dicumarol and arsenate. It was also inhibited by atabrine and Amytal. Antimycin A was effective in partial inhibition of the reversal of electron transfer. In addition malonate and cyanide were found to be potent inhibitors. The mechanism for the generation and utilization of energy for the reversed electron flow, is discussed.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
化学合成中还原力的产生。新硫杆菌中琥珀酸盐的能量链还原吡啶核苷酸
1.1. 本报告中描述的实验表明,琥珀酸盐对新硫杆菌NAD+的还原是能量依赖性的。通过用抗霉素A阻断电子传递链,琥珀酸盐对NAD+的内源性还原需要ATP。吡啶核苷酸的还原涉及黄蛋白系统的中介作用,阿他滨和阿米妥抑制了这一过程。添加的哺乳动物细胞色素c已被证明与T. novellus的电子传递链偶联,从而在没有无机磷酸盐的情况下影响催化生成耦合琥珀酸氧化的高能中间体。因此,非磷酸化的高能化合物可以在偶联位点II上产生,在厌氧条件下,琥珀酸盐与细胞色素c作为电子受体氧化,或者在有氧条件下,在II和III位点上产生,或者在III位点上,通过呼吸链的细胞色素氧化酶部分将电子传递到分子氧,通过细胞色素c氧化产生。在所有情况下,NAD+的还原都是由产生的高能中间体驱动的,涉及细胞色素c水平的电子转移的逆转。琥珀酸盐对NAD+的能量依赖性还原涉及细胞色素c水平电子转移的逆转,对2,4-二硝基苯酚、双酚醇和砷酸盐敏感。阿他滨和阿米妥也能抑制。抗霉素A对电子转移逆转有部分抑制作用。此外,丙二酸盐和氰化物被发现是有效的抑制剂。讨论了反电子流能量的产生和利用机理。
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 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Author index Subject index Insect extramitochondrial glycerophosphate dehydrogenase II. Enzymic properties and amino acid composition of the enzyme from honeybee (Apis mellifera) thoraces The inter-relationships of low redox potential cytochrome c552 and hydrogenase in facultative anaerobes The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1