spacer
spacer

PDBsum entry 1qlb
Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
1qlb

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
655 a.a. *
239 a.a. *
254 a.a. *
Ligands
FAD ×2
FUM ×2
FES ×2
F3S ×2
SF4 ×2
HEM ×4
LMT ×2
Metals
_CA ×2
Waters ×504
* Residue conservation analysis
PDB id:
1qlb
Name: Oxidoreductase
Title: Respiratory complex ii-like fumarate reductase from wolinella succinogenes
Structure: Fumarate reductase flavoprotein subunit. Chain: a, d. Other_details: 8-alpha-[-n-epsilon-histidyl] covalent bond between flavin adenine dinucleotide (fad) and his 43. Fumarate reductase iron-sulfur protein. Chain: b, e. Fumarate reductase cytochrome b subunit. Chain: c, f. Other_details: haem axial ligands - his 44, his 93, his 143, his 182
Source: Wolinella succinogenes. Organism_taxid: 844. Organism_taxid: 844
Biol. unit: Hexamer (from PQS)
Resolution:
2.33Å     R-factor:   0.213     R-free:   0.223
Authors: C.R.D.Lancaster,A.Kroeger,M.Auer,H.Michel
Key ref:
C.R.Lancaster et al. (1999). Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution. Nature, 402, 377-385. PubMed id: 10586875 DOI: 10.1038/46483
Date:
25-Aug-99     Release date:   29-Nov-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P17412  (FRDA_WOLSU) -  Fumarate reductase flavoprotein subunit from Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC 11488 / FDC 602W)
Seq:
Struc: 		 
Seq:
Struc: 		656 a.a.
655 a.a.*
Protein chains
Pfam   ArchSchema ?
P17596  (FRDB_WOLSU) -  Fumarate reductase iron-sulfur subunit from Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC 11488 / FDC 602W)
Seq:
Struc: 		239 a.a.
239 a.a.
Protein chains
Pfam   ArchSchema ?
P17413  (FRDC_WOLSU) -  Fumarate reductase cytochrome b subunit from Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC 11488 / FDC 602W)
Seq:
Struc: 		256 a.a.
254 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B, D, E: E.C.1.3.5.1  - succinate dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Citric acid cycle
      Reaction: a quinone + succinate = fumarate + a quinol
quinone
 +
succinate
Bound ligand (Het Group name = FUM)
corresponds exactly 		= fumarate
 + quinol
      Cofactor: FAD; Iron-sulfur
FAD
Bound ligand (Het Group name = FAD) corresponds exactly 		Iron-sulfur
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1038/46483 Nature 402:377-385 (1999)
PubMed id: 10586875  
 
 
Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution.
C.R.Lancaster, A.Kröger, M.Auer, H.Michel.
 
  ABSTRACT  
 
Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase). Here we describe the crystal structure at 2.2 A resolution of the three protein subunits containing fumarate reductase from the anaerobic bacterium Wolinella succinogenes. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules. On the basis of the structure, we propose a pathway of electron transfer from the dihaem cytochrome b to the site of fumarate reduction and a mechanism of fumarate reduction. The relative orientations of the soluble and membrane-embedded subunits of succinate:quinone oxidoreductases appear to be unique.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Representative parts of the experimental electron-density maps for crystal form A calculated with the MIRAS phases after density modification and phase extension to 2.2 ? resolution. C, N, O, P and S atoms are shown in grey, blue, red, light green and green, respectively; haem iron centres are shown in orange. Contour levels are 1.0 (green) and 9.0 (red) above the mean density of the map. Figs 1-4 and 6 were prepared with a version of Molscript46 modified by R. Esnouf for colour ramping47 and map drawing48 capabilities. a, b, The two haem b molecules (b[P] in the top half; b[D] in the bottom half of each panel) and the side chains of some neighbouring residues in the transmembrane region. c, The covalently bound FAD prosthetic group. 		Figure 2.
Figure 2 The three-dimensional structure of fumarate reductase. a, The fumarate reductase dimer viewed parallel to the membrane. The polypeptide backbones of the two A subunits are shown in blue and light blue, those of the two B subunits in red and pink, and those of the C subunits in green and yellow. Subunit A contains a covalently bound FAD. Subunit B contains three iron-sulphur clusters (Fe[2]S[2], Fe[4]S[4] and Fe[3]S[4]). The membrane-embedded subunit C contains two haem b molecules. b, View of the transmembrane helices of the subunit C dimer along the membrane normal from the cytoplasmic side. One monomer is colour-coded from blue (N terminus) to yellow (C terminus), the other from yellow (N terminus) to red (C terminus)). The transmembrane helices are labelled I, II, IV, V and VI (ref. 22). Secondary structures were assigned using DSSP49. Figure rendered with Raster3D^50.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (1999, 402, 377-385) copyright 1999.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20938980 K.Illergård, A.Kauko, and A.Elofsson (2011).
Why are polar residues within the membrane core evolutionary conserved?
  Proteins, 79, 79-91.  
21307570 T.Kurihara (2011).
A mechanistic analysis of enzymatic degradation of organohalogen compounds.
  Biosci Biotechnol Biochem, 75, 189-198.  
20422082 C.M.Paquete, and R.O.Louro (2010).
Molecular details of multielectron transfer: the case of multiheme cytochromes from metal respiring organisms.
  Dalton Trans, 39, 4259-4266.  
20667175 K.R.Vinothkumar, and R.Henderson (2010).
Structures of membrane proteins.
  Q Rev Biophys, 43, 65.  
20544970 L.J.Smith, A.Kahraman, and J.M.Thornton (2010).
Heme proteins--diversity in structural characteristics, function, and folding.
  Proteins, 78, 2349-2368.  
20331424 N.V.Azarkina, and A.A.Konstantinov (2010).
Energization of Bacillus subtilis membrane vesicles increases catalytic activity of succinate:menaquinone oxidoreductase.
  Biochemistry (Mosc), 75, 50-62.  
20238132 W.Q.Chen, A.Salmazo, M.Myllykoski, B.Sjöblom, M.Bidlingmaier, A.Pollak, P.Baumgärtel, K.Djinovic-Carugo, P.Kursula, and G.Lubec (2010).
Purification of recombinant growth hormone by clear native gels for conformational analyses: preservation of conformation and receptor binding.
  Amino Acids, 39, 859-869.  
19170876 H.D.Juhnke, H.Hiltscher, H.R.Nasiri, H.Schwalbe, and C.R.Lancaster (2009).
Production, characterization and determination of the real catalytic properties of the putative 'succinate dehydrogenase' from Wolinella succinogenes.
  Mol Microbiol, 71, 1088-1101.  
19710024 J.Ruprecht, V.Yankovskaya, E.Maklashina, S.Iwata, and G.Cecchini (2009).
Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site.
  J Biol Chem, 284, 29836-29846.
PDB codes: 2wdq 2wdr 2wdv
18716621 D.S.Lee, P.Nioche, M.Hamberg, and C.S.Raman (2008).
Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes.
  Nature, 455, 363-368.
PDB codes: 2rch 2rcl 2rcm 3cli 3dsi 3dsj 3dsk
18418633 E.A.Berry, and F.A.Walker (2008).
Bis-histidine-coordinated hemes in four-helix bundles: how the geometry of the bundle controls the axial imidazole plane orientations in transmembrane cytochromes of mitochondrial complexes II and III and related proteins.
  J Biol Inorg Chem, 13, 481-498.  
17992543 J.Meyer (2008).
Iron-sulfur protein folds, iron-sulfur chemistry, and evolution.
  J Biol Inorg Chem, 13, 157-170.  
18536726 M.Jormakka, K.Yokoyama, T.Yano, M.Tamakoshi, S.Akimoto, T.Shimamura, P.Curmi, and S.Iwata (2008).
Molecular mechanism of energy conservation in polysulfide respiration.
  Nat Struct Mol Biol, 15, 730-737.
PDB codes: 2vpw 2vpx 2vpy 2vpz
18385138 T.M.Tomasiak, E.Maklashina, G.Cecchini, and T.M.Iverson (2008).
A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II.
  J Biol Chem, 283, 15460-15468.
PDB code: 3cir
18501187 W.Liu, C.E.Rogge, G.F.da Silva, V.P.Shinkarev, A.L.Tsai, Y.Kamensky, G.Palmer, and R.J.Kulmacz (2008).
His92 and His110 selectively affect different heme centers of adrenal cytochrome b(561).
  Biochim Biophys Acta, 1777, 1218-1228.  
17242410 J.D.Otero-Cruz, C.A.Báez-Pagán, I.M.Caraballo-González, and J.A.Lasalde-Dominicci (2007).
Tryptophan-scanning mutagenesis in the alphaM3 transmembrane domain of the muscle-type acetylcholine receptor. A spring model revealed.
  J Biol Chem, 282, 9162-9171.  
17534481 X.Liang, D.J.Campopiano, and P.J.Sadler (2007).
Metals in membranes.
  Chem Soc Rev, 36, 968-992.  
16761086 A.Y.Mulkidjanian, and D.A.Cherepanov (2006).
Probing biological interfaces by tracing proton passage across them.
  Photochem Photobiol Sci, 5, 577-587.  
16829675 E.Maklashina, P.Hellwig, R.A.Rothery, V.Kotlyar, Y.Sher, J.H.Weiner, and G.Cecchini (2006).
Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli.
  J Biol Chem, 281, 26655-26664.  
16484232 E.Maklashina, T.M.Iverson, Y.Sher, V.Kotlyar, J.Andréll, O.Mirza, J.M.Hudson, F.A.Armstrong, R.A.Rothery, J.H.Weiner, and G.Cecchini (2006).
Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain.
  J Biol Chem, 281, 11357-11365.
PDB code: 2b76
16385034 J.E.Butler, R.H.Glaven, A.Esteve-Núñez, C.Núñez, E.S.Shelobolina, D.R.Bond, and D.R.Lovley (2006).
Genetic characterization of a single bifunctional enzyme for fumarate reduction and succinate oxidation in Geobacter sulfurreducens and engineering of fumarate reduction in Geobacter metallireducens.
  J Bacteriol, 188, 450-455.  
17050691 J.Zhang, F.E.Frerman, and J.J.Kim (2006).
Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool.
  Proc Natl Acad Sci U S A, 103, 16212-16217.
PDB codes: 2gmh 2gmj
16699170 K.L.Pankhurst, C.G.Mowat, E.L.Rothery, J.M.Hudson, A.K.Jones, C.S.Miles, M.D.Walkinshaw, F.A.Armstrong, G.A.Reid, and S.K.Chapman (2006).
A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina.
  J Biol Chem, 281, 20589-20597.
PDB codes: 2b7r 2b7s
16371358 L.S.Huang, G.Sun, D.Cobessi, A.C.Wang, J.T.Shen, E.Y.Tung, V.E.Anderson, and E.A.Berry (2006).
3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme.
  J Biol Chem, 281, 5965-5972.
PDB codes: 1yq3 1yq4 2fbw
16935256 L.S.Huang, J.T.Shen, A.C.Wang, and E.A.Berry (2006).
Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the "oxaloacetate-inhibited" state.
  Biochim Biophys Acta, 1757, 1073-1083.
PDB codes: 2h88 2h89
17024183 M.G.Madej, H.R.Nasiri, N.S.Hilgendorff, H.Schwalbe, and C.R.Lancaster (2006).
Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex.
  EMBO J, 25, 4963-4970.
PDB code: 2bs2
16407191 R.Horsefield, V.Yankovskaya, G.Sexton, W.Whittingham, K.Shiomi, S.Omura, B.Byrne, G.Cecchini, and S.Iwata (2006).
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.
  J Biol Chem, 281, 7309-7316.
PDB codes: 2acz 2ad0
16433558 T.Teschner, L.Yatsunyk, V.Schünemann, H.Paulsen, H.Winkler, C.Hu, W.R.Scheidt, F.A.Walker, and A.X.Trautwein (2006).
Models of the membrane-bound cytochromes: mössbauer spectra of crystalline low-spin ferriheme complexes having axial ligand plane dihedral angles ranging from 0 degree to 90 degrees.
  J Am Chem Soc, 128, 1379-1389.  
15781461 A.Kurata, T.Kurihara, H.Kamachi, and N.Esaki (2005).
2-Haloacrylate reductase, a novel enzyme of the medium chain dehydrogenase/reductase superfamily that catalyzes the reduction of a carbon-carbon double bond of unsaturated organohalogen compounds.
  J Biol Chem, 280, 20286-20291.  
16380425 C.R.Lancaster, U.S.Sauer, R.Gross, A.H.Haas, J.Graf, H.Schwalbe, W.Mäntele, J.Simon, and M.G.Madej (2005).
Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase.
  Proc Natl Acad Sci U S A, 102, 18860-18865.
PDB codes: 2bs3 2bs4
15989954 F.Sun, X.Huo, Y.Zhai, A.Wang, J.Xu, D.Su, M.Bartlam, and Z.Rao (2005).
Crystal structure of mitochondrial respiratory membrane protein complex II.
  Cell, 121, 1043-1057.
PDB codes: 1zoy 1zp0
15654871 R.A.Rothery, A.M.Seime, A.M.Spiers, E.Maklashina, I.Schröder, R.P.Gunsalus, G.Cecchini, and J.H.Weiner (2005).
Defining the Q-site of Escherichia coli fumarate reductase by site-directed mutagenesis, fluorescence quench titrations and EPR spectroscopy.
  FEBS J, 272, 313-326.  
15906144 S.T.Ohnishi, T.Ohnishi, S.Muranaka, H.Fujita, H.Kimura, K.Uemura, K.Yoshida, and K.Utsumi (2005).
A possible site of superoxide generation in the complex I segment of rat heart mitochondria.
  J Bioenerg Biomembr, 37, 1.  
15883782 T.Kurokawa, and J.Sakamoto (2005).
Purification and characterization of succinate:menaquinone oxidoreductase from Corynebacterium glutamicum.
  Arch Microbiol, 183, 317-324.  
16245325 W.Iwasaki, H.Miyatake, and K.Miki (2005).
Crystal structure of the small form of glucose-inhibited division protein A from Thermus thermophilus HB8.
  Proteins, 61, 1121-1126.
PDB code: 2cul
14681400 A.Andreeva, D.Howorth, S.E.Brenner, T.J.Hubbard, C.Chothia, and A.G.Murzin (2004).
SCOP database in 2004: refinements integrate structure and sequence family data.
  Nucleic Acids Res, 32, D226-D229.  
15361415 A.H.Haas, and C.R.Lancaster (2004).
Calculated coupling of transmembrane electron and proton transfer in dihemic quinol:fumarate reductase.
  Biophys J, 87, 4298-4315.  
14672929 K.S.Oyedotun, and B.D.Lemire (2004).
The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies.
  J Biol Chem, 279, 9424-9431.
PDB codes: 1orz 1pb4
14672930 K.S.Oyedotun, P.F.Yau, and B.D.Lemire (2004).
Identification of the heme axial ligands in the cytochrome b562 of the Saccharomyces cerevisiae succinate dehydrogenase.
  J Biol Chem, 279, 9432-9439.  
15465852 M.Gimpelev, L.R.Forrest, D.Murray, and B.Honig (2004).
Helical packing patterns in membrane and soluble proteins.
  Biophys J, 87, 4075-4086.  
15048835 R.Das, and M.Gerstein (2004).
A method using active-site sequence conservation to find functional shifts in protein families: application to the enzymes of central metabolism, leading to the identification of an anomalous isocitrate dehydrogenase in pathogens.
  Proteins, 55, 455-463.  
14576151 R.Gross, R.Pisa, M.Sänger, C.R.Lancaster, and J.Simon (2004).
Characterization of the menaquinone reduction site in the diheme cytochrome b membrane anchor of Wolinella succinogenes NiFe-hydrogenase.
  J Biol Chem, 279, 274-281.  
15498942 T.J.Stevens, K.Mizuguchi, and I.T.Arkin (2004).
Distinct protein interfaces in transmembrane domains suggest an in vivo folding model.
  Protein Sci, 13, 3028-3037.  
12885673 D.A.Cherepanov, B.A.Feniouk, W.Junge, and A.Y.Mulkidjanian (2003).
Low dielectric permittivity of water at the membrane interface: effect on the energy coupling mechanism in biological membranes.
  Biophys J, 85, 1307-1316.  
14527321 G.Cecchini (2003).
Function and structure of complex II of the respiratory chain.
  Annu Rev Biochem, 72, 77.  
12694200 H.Miyadera, A.Hiraishi, H.Miyoshi, K.Sakamoto, R.Mineki, K.Murayama, K.V.Nagashima, K.Matsuura, S.Kojima, and K.Kita (2003).
Complex II from phototrophic purple bacterium Rhodoferax fermentans displays rhodoquinol-fumarate reductase activity.
  Eur J Biochem, 270, 1863-1874.  
12515859 H.Miyadera, K.Shiomi, H.Ui, Y.Yamaguchi, R.Masuma, H.Tomoda, H.Miyoshi, A.Osanai, K.Kita, and S.Omura (2003).
Atpenins, potent and specific inhibitors of mitochondrial complex II (succinate-ubiquinone oxidoreductase).
  Proc Natl Acad Sci U S A, 100, 473-477.  
13129931 J.Guo, and B.D.Lemire (2003).
The ubiquinone-binding site of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase is a source of superoxide.
  J Biol Chem, 278, 47629-47635.  
12560540 L.Hederstedt (2003).
Structural biology. Complex II is complex too.
  Science, 299, 671-672.  
12910261 M.G.Bertero, R.A.Rothery, M.Palak, C.Hou, D.Lim, F.Blasco, J.H.Weiner, and N.C.Strynadka (2003).
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A.
  Nat Struct Biol, 10, 681-687.
PDB code: 1q16
14622288 M.H.Hefti, J.Vervoort, and W.J.van Berkel (2003).
Deflavination and reconstitution of flavoproteins.
  Eur J Biochem, 270, 4227-4242.  
14627735 M.J.Lemieux, J.Song, M.J.Kim, Y.Huang, A.Villa, M.Auer, X.D.Li, and D.N.Wang (2003).
Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily.
  Protein Sci, 12, 2748-2756.  
12948771 M.Jormakka, B.Byrne, and S.Iwata (2003).
Formate dehydrogenase--a versatile enzyme in changing environments.
  Curr Opin Struct Biol, 13, 418-423.  
12560550 V.Yankovskaya, R.Horsefield, S.Törnroth, C.Luna-Chavez, H.Miyoshi, C.Léger, B.Byrne, G.Cecchini, and S.Iwata (2003).
Architecture of succinate dehydrogenase and reactive oxygen species generation.
  Science, 299, 700-704.
PDB codes: 1nek 1nen
12594918 W.Martin, and M.J.Russell (2003).
On the origins of cells: a hypothesis for the evolutionary transitions from abiotic geochemistry to chemoautotrophic prokaryotes, and from prokaryotes to nucleated cells.
  Philos Trans R Soc Lond B Biol Sci, 358, 59.  
14674777 Z.Li, J.E.Shokes, A.Kounosu, T.Imai, T.Iwasaki, and R.A.Scott (2003).
X-ray absorption spectroscopic analysis of reductive [2Fe-2S] cluster degradation in hyperthermophilic archaeal succinate:caldariellaquinone oxidoreductase subunits.
  Biochemistry, 42, 15003-15008.  
11939777 A.Brigé, D.Leys, T.E.Meyer, M.A.Cusanovich, and J.J.Van Beeumen (2002).
The 1.25 A resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement.
  Biochemistry, 41, 4827-4836.
PDB code: 1jni
12417132 A.G.Tielens, C.Rotte, J.J.van Hellemond, and W.Martin (2002).
Mitochondria as we don't know them.
  Trends Biochem Sci, 27, 564-572.  
11959503 B.Byrne, and S.Iwata (2002).
Membrane protein complexes.
  Curr Opin Struct Biol, 12, 239-243.  
11846788 C.Schnarrenberger, and W.Martin (2002).
Evolution of the enzymes of the citric acid cycle and the glyoxylate cycle of higher plants. A case study of endosymbiotic gene transfer.
  Eur J Biochem, 269, 868-883.  
11884738 D.Richardson, and G.Sawers (2002).
Structural biology. PMF through the redox loop.
  Science, 295, 1842-1843.  
11842205 G.Fritz, A.Roth, A.Schiffer, T.Büchert, G.Bourenkov, H.D.Bartunik, H.Huber, K.O.Stetter, P.M.Kroneck, and U.Ermler (2002).
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution.
  Proc Natl Acad Sci U S A, 99, 1836-1841.
PDB codes: 1jnr 1jnz
12165429 J.Simon (2002).
Enzymology and bioenergetics of respiratory nitrite ammonification.
  FEMS Microbiol Rev, 26, 285-309.  
11933067 L.Adamian, and J.Liang (2002).
Interhelical hydrogen bonds and spatial motifs in membrane proteins: polar clamps and serine zippers.
  Proteins, 47, 209-218.  
12107136 M.J.Sellars, S.J.Hall, and D.J.Kelly (2002).
Growth of Campylobacter jejuni supported by respiration of fumarate, nitrate, nitrite, trimethylamine-N-oxide, or dimethyl sulfoxide requires oxygen.
  J Bacteriol, 184, 4187-4196.  
11884747 M.Jormakka, S.Törnroth, B.Byrne, and S.Iwata (2002).
Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.
  Science, 295, 1863-1868.
PDB codes: 1kqf 1kqg
12218020 N.Azarkina, and A.A.Konstantinov (2002).
Stimulation of menaquinone-dependent electron transfer in the respiratory chain of Bacillus subtilis by membrane energization.
  J Bacteriol, 184, 5339-5347.  
11856340 O.Hucke, R.Schmid, and A.Labahn (2002).
Exploring the primary electron acceptor (QA)-site of the bacterial reaction center from Rhodobacter sphaeroides. Binding mode of vitamin K derivatives.
  Eur J Biochem, 269, 1096-1108.  
11988468 R.H.Spencer, and D.C.Rees (2002).
The alpha-helix and the organization and gating of channels.
  Annu Rev Biophys Biomol Struct, 31, 207-233.  
11863440 R.T.Bossi, A.Negri, G.Tedeschi, and A.Mattevi (2002).
Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis.
  Biochemistry, 41, 3018-3024.
PDB codes: 1knp 1knr
11952800 S.Biel, J.Simon, R.Gross, T.Ruiz, M.Ruitenberg, and A.Kröger (2002).
Reconstitution of coupled fumarate respiration in liposomes by incorporating the electron transport enzymes isolated from Wolinella succinogenes.
  Eur J Biochem, 269, 1974-1983.  
12167658 T.Iwasaki, A.Kounosu, M.Aoshima, D.Ohmori, T.Imai, A.Urushiyama, N.J.Cosper, and R.A.Scott (2002).
Novel [2Fe-2S]-type redox center C in SdhC of archaeal respiratory complex II from Sulfolobus tokodaii strain 7.
  J Biol Chem, 277, 39642-39648.  
11850430 T.M.Iverson, C.Luna-Chavez, L.R.Croal, G.Cecchini, and D.C.Rees (2002).
Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.
  J Biol Chem, 277, 16124-16130.
PDB codes: 1kf6 1kfy 1l0v
11856339 W.Dietrich, and O.Klimmek (2002).
The function of methyl-menaquinone-6 and polysulfide reductase membrane anchor (PsrC) in polysulfide respiration of Wolinella succinogenes.
  Eur J Biochem, 269, 1086-1095.  
12223076 Z.Ge (2002).
Potential of fumarate reductase as a novel therapeutic target in Helicobacter pylori infection.
  Expert Opin Ther Targets, 6, 135-146.  
11425747 A.I.Tsapin, I.Vandenberghe, K.H.Nealson, J.H.Scott, T.E.Meyer, M.A.Cusanovich, E.Harada, T.Kaizu, H.Akutsu, D.Leys, and J.J.Van Beeumen (2001).
Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1.
  Appl Environ Microbiol, 67, 3236-3244.  
11340051 B.E.Schultz, and S.I.Chan (2001).
Structures and proton-pumping strategies of mitochondrial respiratory enzymes.
  Annu Rev Biophys Biomol Struct, 30, 23-65.  
11248702 C.R.Lancaster, R.Gross, and J.Simon (2001).
A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction.
  Eur J Biochem, 268, 1820-1827.
PDB code: 1e7p
11761328 D.E.Edmondson, and P.Newton-Vinson (2001).
The covalent FAD of monoamine oxidase: structural and functional role and mechanism of the flavinylation reaction.
  Antioxid Redox Signal, 3, 789-806.  
11294641 G.Tedeschi, S.Ronchi, T.Simonic, C.Treu, A.Mattevi, and A.Negri (2001).
Probing the active site of L-aspartate oxidase by site-directed mutagenesis: role of basic residues in fumarate reduction.
  Biochemistry, 40, 4738-4744.  
11406389 I.Ubarretxena-Belandia, and D.M.Engelman (2001).
Helical membrane proteins: diversity of functions in the context of simple architecture.
  Curr Opin Struct Biol, 11, 370-376.  
11358526 M.Schnorpfeil, I.G.Janausch, S.Biel, A.Kröger, and G.Unden (2001).
Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase.
  Eur J Biochem, 268, 3069-3074.  
11746826 R.J.Bienstock, and J.C.Barrett (2001).
KAI1, a prostate metastasis suppressor: prediction of solvated structure and interactions with binding partners; integrins, cadherins, and cell-surface receptor proteins.
  Mol Carcinog, 32, 139-153.  
10975456 A.W.Munro, P.Taylor, and M.D.Walkinshaw (2000).
Structures of redox enzymes.
  Curr Opin Biotechnol, 11, 369-376.  
11188694 C.Binda, R.T.Bossi, S.Wakatsuki, S.Arzt, A.Coda, B.Curti, M.A.Vanoni, and A.Mattevi (2000).
Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase.
  Structure, 8, 1299-1308.
PDB code: 1ea0
11004459 C.R.Lancaster, and A.Kröger (2000).
Succinate: quinone oxidoreductases: new insights from X-ray crystal structures.
  Biochim Biophys Acta, 1459, 422-431.  
11186225 C.R.Lancaster, R.Gorss, A.Haas, M.Ritter, W.Mäntele, J.Simon, and A.Kröger (2000).
Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductase.
  Proc Natl Acad Sci U S A, 97, 13051-13056.  
11004445 G.A.Reid, C.S.Miles, R.K.Moysey, K.L.Pankhurst, and S.K.Chapman (2000).
Catalysis in fumarate reductase.
  Biochim Biophys Acta, 1459, 310-315.  
10966478 J.L.Popot, and D.M.Engelman (2000).
Helical membrane protein folding, stability, and evolution.
  Annu Rev Biochem, 69, 881-922.  
10978153 M.K.Doherty, S.L.Pealing, C.S.Miles, R.Moysey, P.Taylor, M.D.Walkinshaw, G.A.Reid, and S.K.Chapman (2000).
Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study.
  Biochemistry, 39, 10695-10701.
PDB code: 1e39
10913269 M.Matsson, D.Tolstoy, R.Aasa, and L.Hederstedt (2000).
The distal heme center in Bacillus subtilis succinate:quinone reductase is crucial for electron transfer to menaquinone.
  Biochemistry, 39, 8617-8624.  
11090820 M.le Maire, P.Champeil, and J.V.Moller (2000).
Interaction of membrane proteins and lipids with solubilizing detergents.
  Biochim Biophys Acta, 1508, 86.  
10956051 R.Camba, and F.A.Armstrong (2000).
Investigations of the oxidative disassembly of Fe-S clusters in Clostridium pasteurianum 8Fe ferredoxin using pulsed-protein-film voltammetry.
  Biochemistry, 39, 10587-10598.  
11004174 R.Ullmann, R.Gross, J.Simon, G.Unden, and A.Kröger (2000).
Transport of C(4)-dicarboxylates in Wolinella succinogenes.
  J Bacteriol, 182, 5757-5764.  
10981634 T.M.Iverson, C.Luna-Chavez, I.Schröder, G.Cecchini, and D.C.Rees (2000).
Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex.
  Curr Opin Struct Biol, 10, 448-455.  
10673443 T.Ohnishi, C.C.Moser, C.C.Page, P.L.Dutton, and T.Yano (2000).
Simple redox-linked proton-transfer design: new insights from structures of quinol-fumarate reductase.
  Structure, 8, R23-R32.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

spacer
spacer