DOI: 10.1126/science.1068186. Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N

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

10.1126/science.1068186

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

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.

Bibliography

Jormakka, M., ToÌrnroth, S., Byrne, B., & Iwata, S. (2002). Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N. Science, 295(5561), 1863â1868.

Authors 4

Mika Jormakka (first)
Susanna Törnroth (additional)
Bernadette Byrne (additional)
So Iwata (additional)

References 36 Referenced 436

For a review see
10.1126/science.283.5407.1488
10.1016/0022-5193(76)90124-7
For a review see
10.1016/0005-2728(95)00092-5
For a review see
10.1099/00221287-146-3-551
For a review see
10.1007/PL00000846
10.1111/j.1574-6968.1980.tb05072.x
10.1016/S0021-9258(18)54583-X
Supplementary material is available on Science Online at www.sciencemag.org/cgi/content/295/5561/1863/DC1.
10.1111/j.1365-2958.1995.tb02246.x
10.1128/JB.180.24.6625-6634.1998
10.1126/science.275.5304.1305
10.1038/46972
10.1074/jbc.273.13.7462
For a review see
10.1146/annurev.biochem.66.1.233
10.1126/science.272.5268.1615
10.1016/S0969-2126(99)80010-0
10.1107/S0108767390010224
10.1021/bi972177k
10.1038/235040a0
10.1111/j.1432-1033.1992.tb17020.x
10.1046/j.1365-2958.1998.01100.x
L. Meek D. J. Arp. J. Bacteriol. 182 3429 (2000). (10.1128/JB.182.12.3429-3436.2000)
10.1111/j.1432-1033.1979.tb12914.x
10.1126/science.281.5373.64
10.1038/46483
S. Biel et al. Eur. J. Biochem. in press.
M. Jormakka S. Törnroth B. Byrne S. Iwata data not shown.
10.1107/S0021889891004399
Esnouf R., J. Mol. Graph. 15, 133 (1997). / J. Mol. Graph. by Esnouf R. (1997)
10.1107/S0907444994006396
The research was supported by the Biotechnology and Biological Sciences Research Council of the UK and the Structural Biology Network of Sweden. We thank E. Mitchell and A. Thompson at the European Synchrotron Radiation Facility Grenoble for technical assistance J. Barber B. C. Berks R.C. Lancaster F. Sargent J. Butt J. Simon C. Page and P. L. Dutton for critical assessment of this manuscript. The coordinates for the native Fdh-N and the HQNO complex are deposited with the PDB (entries 1KQF and 1KQG respectively).

Dates

Type	When
Created	23 years ago (July 27, 2002, 5:35 a.m.)
Deposited	1 year, 7 months ago (Jan. 9, 2024, 10:32 p.m.)
Indexed	3 weeks, 2 days ago (July 30, 2025, 10:22 a.m.)
Issued	23 years, 5 months ago (March 8, 2002)
Published	23 years, 5 months ago (March 8, 2002)
Published Print	23 years, 5 months ago (March 8, 2002)

Funders 0

None

BibTeX

@article{Jormakka_2002, title={Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N}, volume={295}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1068186}, DOI={10.1126/science.1068186}, number={5561}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Jormakka, Mika and Törnroth, Susanna and Byrne, Bernadette and Iwata, So}, year={2002}, month=mar, pages={1863–1868} }

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