Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N
Mika Jormakka,1Susanna Törnroth,3Bernadette Byrne,2So Iwata123*
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
demonstrates11 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 extendsalmost 90 angstroms through the enzyme. The
menaquinone reductionsite associated with a possible proton pathway
was also characterized.This structure provides critical insights into
the proton motiveforce generation by redox loop, a common mechanism
among a widerange of respiratory enzymes.
1 Division of Biomedical Sciences and
2 Department of Biological Sciences, Imperial
College, London SW7 2AZ, UK.
3 Department of
Biochemistry, BMC, Uppsala University, Box 576, S-75123 Uppsala,
Sweden.
*
To whom correspondence should be addressed. E-mail:
s.iwata{at}ic.ac.uk
The editors suggest the following Related Resources on Science sites:
In Science Magazine
PERSPECTIVES
David Richardson and Gary Sawers (8 March 2002) Science295 (5561), 1842.
[DOI: 10.1126/science.1070366] |Summary »|Full Text »|PDF »
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A Molybdopterin Oxidoreductase Is Involved in H2 Oxidation in Desulfovibrio desulfuricans G20.
X. Li, Q. Luo, N. Q. Wofford, K. L. Keller, M. J. McInerney, J. D. Wall, and L. R. Krumholz (2009)
J. Bacteriol.
191, 2675-2682
|Abstract »|Full Text »|PDF »
Formate-Dependent Autotrophic Growth in Sinorhizobium meliloti.
Evolutionary Persistence of the Molybdopyranopterin-Containing Sulfite Oxidase Protein Fold.
G. J. Workun, K. Moquin, R. A. Rothery, and J. H. Weiner (2008)
Microbiol. Mol. Biol. Rev.
72, 228-248
|Abstract »|Full Text »|PDF »
Histidine Cycle Mechanism for the Concerted Proton/Electron Transfer from Ascorbate to the Cytosolic Haem b Centre of Cytochrome b561: A Unique Machinery for the Biological Transmembrane Electron Transfer.
Spectropotentiometric and Structural Analysis of the Periplasmic Nitrate Reductase from Escherichia coli.
B. J. N. Jepson, S. Mohan, T. A. Clarke, A. J. Gates, J. A. Cole, C. S. Butler, J. N. Butt, A. M. Hemmings, and D. J. Richardson (2007)
J. Biol. Chem.
282, 6425-6437
|Abstract »|Full Text »|PDF »
Constructing the wonders of the bacterial world: biosynthesis of complex enzymes.
Soluble Aldose Sugar Dehydrogenase from Escherichia coli: A HIGHLY EXPOSED ACTIVE SITE CONFERRING BROAD SUBSTRATE SPECIFICITY.
S. M. Southall, J. J. Doel, D. J. Richardson, and A. Oubrie (2006)
J. Biol. Chem.
281, 30650-30659
|Abstract »|Full Text »|PDF »
Resolution of Distinct Membrane-Bound Enzymes from Enterobacter cloacae SLD1a-1 That Are Responsible for Selective Reduction of Nitrate and Selenate Oxyanions.
H. Ridley, C. A. Watts, D. J. Richardson, and C. S. Butler (2006)
Appl. Envir. Microbiol.
72, 5173-5180
|Abstract »|Full Text »|PDF »
Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria..
T. Zaunmuller, D. J. Kelly, F. O. Glockner, and G. Unden (2006)
Microbiology
152, 2443-2453
|Abstract »|Full Text »|PDF »
Reduction of Soluble and Insoluble Iron Forms by Membrane Fractions of Shewanella oneidensis Grown under Aerobic and Anaerobic Conditions.
S. S. Ruebush, S. L. Brantley, and M. Tien (2006)
Appl. Envir. Microbiol.
72, 2925-2935
|Abstract »|Full Text »|PDF »
Structural and Computational Analysis of the Quinone-binding Site of Complex II (Succinate-Ubiquinone Oxidoreductase): A MECHANISM OF ELECTRON TRANSFER AND PROTON CONDUCTION DURING UBIQUINONE REDUCTION.
R. Horsefield, V. Yankovskaya, G. Sexton, W. Whittingham, K. Shiomi, S. Omura, B. Byrne, G. Cecchini, and S. Iwata (2006)
J. Biol. Chem.
281, 7309-7316
|Abstract »|Full Text »|PDF »
Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase.
C. R. D. Lancaster, U. S. Sauer, R. Gross, A. H. Haas, J. Graf, H. Schwalbe, W. Mantele, J. Simon, and M. G. Madej (2005)
PNAS
102, 18860-18865
|Abstract »|Full Text »|PDF »
Structural and Biochemical Characterization of a Quinol Binding Site of Escherichia coli Nitrate Reductase A.
M. G. Bertero, R. A. Rothery, N. Boroumand, M. Palak, F. Blasco, N. Ginet, J. H. Weiner, and N. C. J. Strynadka (2005)
J. Biol. Chem.
280, 14836-14843
|Abstract »|Full Text »|PDF »
A Little Help from My Friends: Quality Control of Presecretory Proteins in Bacteria.
A. C. Fisher and M. P. DeLisa (2004)
J. Bacteriol.
186, 7467-7473
|Full Text »|PDF »
Involvement of the Molybdenum Cofactor Biosynthetic Machinery in the Maturation of the Escherichia coli Nitrate Reductase A.
A. Vergnes, K. Gouffi-Belhabich, F. Blasco, G. Giordano, and A. Magalon (2004)
J. Biol. Chem.
279, 41398-41403
|Abstract »|Full Text »|PDF »
mRNA Secondary Structure Modulates Translation of Tat-Dependent Formate Dehydrogenase N.
C. Punginelli, B. Ize, N. R. Stanley, V. Stewart, G. Sawers, B. C. Berks, and T. Palmer (2004)
J. Bacteriol.
186, 6311-6315
|Abstract »|Full Text »|PDF »
Kinetic and Mechanistic Characterization of the Formyl-CoA Transferase from Oxalobacter formigenes.
S. Jonsson, S. Ricagno, Y. Lindqvist, and N. G. J. Richards (2004)
J. Biol. Chem.
279, 36003-36012
|Abstract »|Full Text »|PDF »
Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.
A. Messerschmidt, H. Niessen, D. Abt, O. Einsle, B. Schink, and P. M. H. Kroneck (2004)
PNAS
101, 11571-11576
|Abstract »|Full Text »|PDF »
Computational analysis of {alpha}-helical membrane protein structure: implications for the prediction of 3D structural models.
T. A. Eyre, L. Partridge, and J. M. Thornton (2004)
Protein Eng. Des. Sel.
17, 613-624
|Abstract »|Full Text »|PDF »
Selenocysteine-Containing Proteins in Anaerobic Benzoate Metabolism of Desulfococcus multivorans.
Characterization of the Menaquinone Reduction Site in the Diheme Cytochrome b Membrane Anchor of Wolinella succinogenes NiFe-hydrogenase.
R. Gross, R. Pisa, M. Sanger, C. R. D. Lancaster, and J. Simon (2004)
J. Biol. Chem.
279, 274-281
|Abstract »|Full Text »|PDF »
SCOP database in 2004: refinements integrate structure and sequence family data.
A. Andreeva, D. Howorth, S. E. Brenner, T. J. P. Hubbard, C. Chothia, and A. G. Murzin (2004)
Nucleic Acids Res.
32, D226-229
|Abstract »|Full Text »|PDF »
Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens.
S. Laska, F. Lottspeich, and A. Kletzin (2003)
Microbiology
149, 2357-2371
|Abstract »|Full Text »|PDF »
Arsenite Oxidase, an Ancient Bioenergetic Enzyme.
E. Lebrun, M. Brugna, F. Baymann, D. Muller, D. Lievremont, M.-C. Lett, and W. Nitschke (2003)
Mol. Biol. Evol.
20, 686-693
|Abstract »|Full Text »|PDF »
Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation.
V. Yankovskaya, R. Horsefield, S. Tornroth, C. Luna-Chavez, H. Miyoshi, C. Leger, B. Byrne, G. Cecchini, and S. Iwata (2003)
Science
299, 700-704
|Abstract »|Full Text »|PDF »
Novel [2Fe-2S]-type Redox Center C in SdhC of Archaeal Respiratory Complex II from Sulfolobus tokodaii Strain 7.
T. Iwasaki, A. Kounosu, M. Aoshima, D. Ohmori, T. Imai, A. Urushiyama, N. J. Cosper, and R. A. Scott (2002)
J. Biol. Chem.
277, 39642-39648
|Abstract »|Full Text »|PDF »