Molecular basis of proton motive force generation:: Structure of formate dehydrogenase-N

被引:388
作者
Jormakka, M
Törnroth, S
Byrne, B
Iwata, S [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Div Biomed Sci, London SW7 2AZ, England
[2] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AZ, England
[3] Univ Uppsala, BMC, Dept Biochem, S-75123 Uppsala, Sweden
关键词
D O I
10.1126/science.1068186
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
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收藏
页码:1863 / 1868
页数:6
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