Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N

Author:

Jormakka Mika1,Törnroth Susanna2,Byrne Bernadette3,Iwata So132

Affiliation:

1. Division of Biomedical Sciences and

2. Department of Biochemistry, BMC, Uppsala University, Box 576, S-75123 Uppsala, Sweden.

3. Department of Biological Sciences, Imperial College, London SW7 2AZ, UK.

Abstract

The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Cited by 452 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. The monotopic quinone reductases from Staphylococcus aureus;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2024-11

2. Enzymatic CO2 reduction catalyzed by natural and artificial Metalloenzymes;Journal of Inorganic Biochemistry;2024-10

3. Undulating Free Energy Landscapes Buffer Redox Chains from Environmental Fluctuations;The Journal of Physical Chemistry B;2024-09-08

4. The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions;JBIC Journal of Biological Inorganic Chemistry;2024-05-23

5. Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase;Acta Crystallographica Section F Structural Biology Communications;2024-05-01

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3