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PDBsum entry 1rie

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Electron transport PDB id
1rie
Jmol
Contents
Protein chain
127 a.a. *
Ligands
FES
Waters ×167
* Residue conservation analysis
PDB id:
1rie
Name: Electron transport
Title: Structure of a water soluble fragment of the rieske iron- sulfur protein of the bovine heart mitochondrial cytochrome bc1-complex
Structure: Rieske iron-sulfur protein. Chain: a. Fragment: soluble fragment. Synonym: ubiquinol-cytochromE C reductase iron-sulfur. Ec: 1.10.2.2
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: heart. Organelle: mitochondria
Resolution:
1.50Å     R-factor:   0.187     R-free:   0.211
Authors: S.Iwata,M.Saynovits,T.A.Link,H.Michel
Key ref:
S.Iwata et al. (1996). Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution. Structure, 4, 567-579. PubMed id: 8736555 DOI: 10.1016/S0969-2126(96)00062-7
Date:
23-Feb-96     Release date:   07-Dec-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13272  (UCRI_BOVIN) -  Cytochrome b-c1 complex subunit Rieske, mitochondrial
Seq:
Struc:
274 a.a.
127 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.10.2.2  - Quinol--cytochrome-c reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
Quinol
+ 2 × ferricytochrome c
= quinone
+ 2 × ferrocytochrome c
+ 2 × H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     oxidoreductase activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1016/S0969-2126(96)00062-7 Structure 4:567-579 (1996)
PubMed id: 8736555  
 
 
Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution.
S.Iwata, M.Saynovits, T.A.Link, H.Michel.
 
  ABSTRACT  
 
BACKGROUND: The 'Rieske' iron-sulfur protein is the primary electron acceptor during hydroquinone oxidation in cytochrome bc complexes. The spectroscopic and electrochemical properties of the 'Rieske' [2Fe-2S] cluster differ significantly from those of other iron-sulfur clusters. A 129-residue water soluble fragment containing the intact [2Fe-2S] cluster was isolated following proteolytic digestion of the bc1 complex and used for structural studies. RESULTS: The structure of the Rieske iron-sulfur fragment containing the reduced [2Fe-2S] cluster has been determined using the multiwavelength anomalous diffraction (MAD) technique and refined at 1.5 A resolution. The fragment has a novel overall fold that includes three sheets of beta strands. The iron atoms of the [2Fe-2S] cluster are coordinated by two cysteine (Fe-1) and two histidine (Fe-2) residues, respectively, with the histidine ligands completely exposed to the solvent. This is in contrast to the four cysteine coordination pattern observed in previously characterised [2Fe-2S] ferredoxins. The cluster-binding fold is formed by two loops connected by a disulfide bridge; these loops superpose with the metal-binding loops of rubredoxins. The environment of the cluster is stabilised by an extensive hydrogen-bond network. CONCLUSIONS: The high-resolution structure supports the proposed coordination pattern involving histidine ligands and provides a basis for a detailed analysis of the spectroscopic and electrochemical properties. As the cluster is located at the tip of the protein, it might come into close contact with cytochrome b. The exposed N epsilon atoms of the histidine ligands of the cluster are readily accessible to quinones and inhibitors within the hydroquinone oxidation (QP) pocket of the bc1 complex and may undergo redox-dependent protonation/deprotonation.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Topology of the ISF. The hydrogen-bond pattern and secondary structure assignment are indicated. The residues conserved in all known Rieske iron–sulfur proteins from cytochrome bc[1] complexes are printed in red. The outlined characters denote residues missing in Rieske iron–sulfur protein from the cytochrome b[6]^f complex. Metal ligands and residues that form a disulfide bridge are colored yellow and green, respectively. Figure 3. Topology of the ISF. The hydrogen-bond pattern and secondary structure assignment are indicated. The residues conserved in all known Rieske iron–sulfur proteins from cytochrome bc[1] complexes are printed in red. The outlined characters denote residues missing in Rieske iron–sulfur protein from the cytochrome b[6]^f complex. Metal ligands and residues that form a disulfide bridge are colored yellow and green, respectively.
Figure 6.
Figure 6. Electrostatic surface properties of the ISF. Molecular surface of ISF color-coded by electrostatic potential: red, negative; blue, positive. The extreme ranges of red and blue represent electrostatic potentials of −5 and +5 k[B]T, respectively (k[B], Boltzmann constant; T, temperature). The view shows the same orientation as Figure 2a. The figure was generated using the program GRASP [50]. Figure 6. Electrostatic surface properties of the ISF. Molecular surface of ISF color-coded by electrostatic potential: red, negative; blue, positive. The extreme ranges of red and blue represent electrostatic potentials of −5 and +5 k[B]T, respectively (k[B], Boltzmann constant; T, temperature). The view shows the same orientation as [3]Figure 2a. The figure was generated using the program GRASP [4][50].
 
  The above figures are reprinted by permission from Cell Press: Structure (1996, 4, 567-579) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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Iron-sulfur world in aerobic and hyperthermoacidophilic archaea Sulfolobus.
  Archaea, 2010, 0.  
20737532 Y.El Khoury, A.Trivella, J.Gross, and P.Hellwig (2010).
Probing the hydrogen bonding structure in the Rieske protein.
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19099453 D.R.Kolling, R.I.Samoilova, A.A.Shubin, A.R.Crofts, and S.A.Dikanov (2009).
Proton environment of reduced Rieske iron-sulfur cluster probed by two-dimensional ESEEM spectroscopy.
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19804777 T.Iwasaki, R.I.Samoilova, A.Kounosu, and S.A.Dikanov (2009).
Two-dimensional pulsed electron spin resonance characterization of 15N-labeled archaeal Rieske-type ferredoxin.
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18766386 Y.El Khoury, and P.Hellwig (2009).
Infrared spectroscopic characterization of copper-polyhistidine from 1,800 to 50 cm(-1): model systems for copper coordination.
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19459625 Z.J.Tonzetich, L.H.Do, and S.J.Lippard (2009).
Dinitrosyl iron complexes relevant to Rieske cluster nitrosylation.
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18703841 E.J.Levin, N.L.Elsen, K.D.Seder, J.G.McCoy, B.G.Fox, and G.N.Phillips (2008).
X-ray structure of a soluble Rieske-type ferredoxin from Mus musculus.
  Acta Crystallogr D Biol Crystallogr, 64, 933-940.
PDB code: 3d89
18719951 E.N.Brown, R.Friemann, A.Karlsson, J.V.Parales, M.M.Couture, L.D.Eltis, and S.Ramaswamy (2008).
Determining Rieske cluster reduction potentials.
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PDB code: 2qpz
18258178 H.W.Ma, S.Yang, L.Yu, and C.A.Yu (2008).
Formation of engineered intersubunit disulfide bond in cytochrome bc1 complex disrupts electron transfer activity in the complex.
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17992543 J.Meyer (2008).
Iron-sulfur protein folds, iron-sulfur chemistry, and evolution.
  J Biol Inorg Chem, 13, 157-170.  
18286376 S.Boxhammer, S.Glaser, A.Kühl, A.K.Wagner, and C.L.Schmidt (2008).
Characterization of the recombinant Rieske [2Fe-2S] proteins HcaC and YeaW from E. coli.
  Biometals, 21, 459-467.  
17349044 D.J.Ferraro, E.N.Brown, C.L.Yu, R.E.Parales, D.T.Gibson, and S.Ramaswamy (2007).
Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1.
  BMC Struct Biol, 7, 10.
PDB codes: 2gbw 2gbx 2i7f
17223530 D.J.Kolling, J.S.Brunzelle, S.Lhee, A.R.Crofts, and S.K.Nair (2007).
Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters.
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PDB codes: 2nuk 2num 2nve 2nvf 2nvg 2nwf
16771672 C.M.Koehler, K.N.Beverly, and E.P.Leverich (2006).
Redox pathways of the mitochondrion.
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16962969 D.P.Kloer, C.Hagel, J.Heider, and G.E.Schulz (2006).
Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum.
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PDB code: 2ivf
16987314 J.Bachmann, B.Bauer, K.Zwicker, B.Ludwig, and O.Anderka (2006).
The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin-arginine translocase.
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16627939 L.A.Moe, C.A.Bingman, G.E.Wesenberg, G.N.Phillips, and B.G.Fox (2006).
Structure of T4moC, the Rieske-type ferredoxin component of toluene 4-monooxygenase.
  Acta Crystallogr D Biol Crystallogr, 62, 476-482.
PDB code: 1vm9
16830148 L.Noodleman, and W.G.Han (2006).
Structure, redox, pKa, spin. A golden tetrad for understanding metalloenzyme energetics and reaction pathways.
  J Biol Inorg Chem, 11, 674-694.  
16854984 S.A.Dikanov, D.R.Kolling, B.Endeward, R.I.Samoilova, T.F.Prisner, S.K.Nair, and A.R.Crofts (2006).
Identification of hydrogen bonds to the Rieske cluster through the weakly coupled nitrogens detected by electron spin echo envelope modulation spectroscopy.
  J Biol Chem, 281, 27416-27425.  
  17012793 T.Iwasaki, A.Kounosu, D.Ohmori, and T.Kumasaka (2006).
Crystallization and preliminary X-ray diffraction studies of a hyperthermophilic Rieske protein variant (SDX-triple) with an engineered rubredoxin-like mononuclear iron site.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 993-995.  
16877714 T.Iwasaki, A.Kounosu, D.R.Kolling, S.Lhee, A.R.Crofts, S.A.Dikanov, T.Uchiyama, T.Kumasaka, H.Ishikawa, M.Kono, T.Imai, and A.Urushiyama (2006).
Resonance Raman characterization of archaeal and bacterial Rieske protein variants with modified hydrogen bond network around the [2Fe-2S] center.
  Protein Sci, 15, 2019-2024.  
16756511 W.A.Cramer, H.Zhang, J.Yan, G.Kurisu, and J.L.Smith (2006).
Transmembrane traffic in the cytochrome b6f complex.
  Annu Rev Biochem, 75, 769-790.  
15983423 H.Bönisch, C.L.Schmidt, P.Bianco, and R.Ladenstein (2005).
Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 A X-ray structure of mutant W4L/R5S.
  Acta Crystallogr D Biol Crystallogr, 61, 990.
PDB codes: 1yk4 1yk5
16150698 J.Lee, M.Simurdiak, and H.Zhao (2005).
Reconstitution and characterization of aminopyrrolnitrin oxygenase, a Rieske N-oxygenase that catalyzes unusual arylamine oxidation.
  J Biol Chem, 280, 36719-36727.  
15645447 J.W.Nam, H.Noguchi, Z.Fujimoto, H.Mizuno, Y.Ashikawa, M.Abo, S.Fushinobu, N.Kobashi, T.Wakagi, K.Iwata, T.Yoshida, H.Habe, H.Yamane, T.Omori, and H.Nojiri (2005).
Crystal structure of the ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-heme iron oxygenase system.
  Proteins, 58, 779-789.
PDB code: 1vck
15989955 N.Mesecke, N.Terziyska, C.Kozany, F.Baumann, W.Neupert, K.Hell, and J.M.Herrmann (2005).
A disulfide relay system in the intermembrane space of mitochondria that mediates protein import.
  Cell, 121, 1059-1069.  
15618217 S.Meier, W.Neupert, and J.M.Herrmann (2005).
Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria.
  J Biol Chem, 280, 7777-7785.  
15632131 T.Iwasaki, A.Kounosu, Y.Tao, Z.Li, J.E.Shokes, N.J.Cosper, T.Imai, A.Urushiyama, and R.A.Scott (2005).
Rational design of a mononuclear metal site into the archaeal Rieske-type protein scaffold.
  J Biol Chem, 280, 9129-9134.  
14726526 A.Kounosu, Z.Li, N.J.Cosper, J.E.Shokes, R.A.Scott, T.Imai, A.Urushiyama, and T.Iwasaki (2004).
Engineering a three-cysteine, one-histidine ligand environment into a new hyperthermophilic archaeal Rieske-type [2Fe-2S] ferredoxin from Sulfolobus solfataricus.
  J Biol Chem, 279, 12519-12528.  
15263097 E.J.Leggate, E.Bill, T.Essigke, G.M.Ullmann, and J.Hirst (2004).
Formation and characterization of an all-ferrous Rieske cluster and stabilization of the [2Fe-2S]0 core by protonation.
  Proc Natl Acad Sci U S A, 101, 10913-10918.  
15452777 L.Skjeldal, F.C.Peterson, J.F.Doreleijers, L.A.Moe, J.D.Pikus, W.M.Westler, J.L.Markley, B.F.Volkman, and B.G.Fox (2004).
Solution structure of T4moC, the Rieske ferredoxin component of the toluene 4-monooxygenase complex.
  J Biol Inorg Chem, 9, 945-953.
PDB code: 1sjg
15294910 S.P.Curran, D.Leuenberger, E.P.Leverich, D.K.Hwang, K.N.Beverly, and C.M.Koehler (2004).
The role of Hot13p and redox chemistry in the mitochondrial TIM22 import pathway.
  J Biol Chem, 279, 43744-43751.  
15272185 T.Uchiyama, A.Kounosu, T.Sato, N.Tanaka, T.Iwasaki, and T.Kumasaka (2004).
Crystallization and preliminary X-ray diffraction studies of the hyperthermophilic archaeal sulredoxin having the unique Rieske [2Fe-2S] cluster environment.
  Acta Crystallogr D Biol Crystallogr, 60, 1487-1489.  
12672829 J.Yan, and W.A.Cramer (2003).
Functional insensitivity of the cytochrome b6f complex to structure changes in the hinge region of the Rieske iron-sulfur protein.
  J Biol Chem, 278, 20925-20933.  
12777806 P.Retailleau, and T.Prangé (2003).
Phasing power at the K absorption edge of organic arsenic.
  Acta Crystallogr D Biol Crystallogr, 59, 887-896.
PDB code: 1n4f
12527760 S.S.Krishna, I.Majumdar, and N.V.Grishin (2003).
Structural classification of zinc fingers: survey and summary.
  Nucleic Acids Res, 31, 532-550.  
11900550 A.G.Roberts, M.K.Bowman, and D.M.Kramer (2002).
Certain metal ions are inhibitors of cytochrome b6f complex 'Rieske' iron-sulfur protein domain movements.
  Biochemistry, 41, 4070-4079.  
12089152 A.P.Yeh, X.I.Ambroggio, S.L.Andrade, O.Einsle, C.Chatelet, J.Meyer, and D.C.Rees (2002).
High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus.
  J Biol Chem, 277, 34499-34507.
PDB codes: 1m2a 1m2b 1m2d
12441394 N.J.Cosper, D.M.Eby, A.Kounosu, N.Kurosawa, E.L.Neidle, D.M.Kurtz, T.Iwasaki, and R.A.Scott (2002).
Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters.
  Protein Sci, 11, 2969-2973.  
11841221 Y.Zhen, B.Schmidt, U.G.Kang, W.Antholine, and S.Ferguson-Miller (2002).
Mutants of the CuA site in cytochrome c oxidase of Rhodobacter sphaeroides: I. Spectral and functional properties.
  Biochemistry, 41, 2288-2297.  
11141059 M.M.Couture, C.L.Colbert, E.Babini, F.I.Rosell, A.G.Mauk, J.T.Bolin, and L.D.Eltis (2001).
Characterization of BphF, a Rieske-type ferredoxin with a low reduction potential.
  Biochemistry, 40, 84-92.  
11250197 P.J.Ellis, T.Conrads, R.Hille, and P.Kuhn (2001).
Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A.
  Structure, 9, 125-132.
PDB codes: 1g8j 1g8k
10632705 A.Kapazoglou, R.M.Mould, and J.C.Gray (2000).
Assembly of the Rieske iron-sulphur protein into the cytochrome bf complex in thylakoid membranes of isolated pea chloroplasts.
  Eur J Biochem, 267, 352-360.  
10727220 B.K.Rao, A.M.Tyryshkin, A.G.Roberts, M.K.Bowman, and D.M.Kramer (2000).
Inhibitory copper binding site on the spinach cytochrome b6f complex: implications for Qo site catalysis.
  Biochemistry, 39, 3285-3296.  
10873857 C.Hunte, J.Koepke, C.Lange, T.Rossmanith, and H.Michel (2000).
Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.
  Structure, 8, 669-684.
PDB code: 1ezv
11188691 C.L.Colbert, M.M.Couture, L.D.Eltis, and J.T.Bolin (2000).
A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins.
  Structure, 8, 1267-1278.
PDB code: 1fqt
10966481 E.A.Berry, M.Guergova-Kuras, L.S.Huang, and A.R.Crofts (2000).
Structure and function of cytochrome bc complexes.
  Annu Rev Biochem, 69, 1005-1075.  
10771436 H.Bönisch, C.L.Schmidt, G.Schäfer, and R.Ladenstein (2000).
Crystallization and preliminary crystallographic analysis of Rieske iron-sulfur protein II (soxF) from sulfolobus acidocaldarius.
  Acta Crystallogr D Biol Crystallogr, 56, 643-644.  
10891064 J.N.Agar, C.Krebs, J.Frazzon, B.H.Huynh, D.R.Dean, and M.K.Johnson (2000).
IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU.
  Biochemistry, 39, 7856-7862.  
10858292 M.Guergova-Kuras, R.Kuras, N.Ugulava, I.Hadad, and A.R.Crofts (2000).
Specific mutagenesis of the rieske iron-sulfur protein in Rhodobacter sphaeroides shows that both the thermodynamic gradient and the pK of the oxidized form determine the rate of quinol oxidation by the bc(1) complex.
  Biochemistry, 39, 7436-7444.  
10869174 Y.I.Chi, L.S.Huang, Z.Zhang, J.G.Fernández-Velasco, and E.A.Berry (2000).
X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii.
  Biochemistry, 39, 7689-7701.
PDB code: 1cfm
10625446 A.R.Crofts, B.Barquera, R.B.Gennis, R.Kuras, M.Guergova-Kuras, and E.A.Berry (1999).
Mechanism of ubiquinol oxidation by the bc(1) complex: different domains of the quinol binding pocket and their role in the mechanism and binding of inhibitors.
  Biochemistry, 38, 15807-15826.  
10625445 A.R.Crofts, M.Guergova-Kuras, L.Huang, R.Kuras, Z.Zhang, and E.A.Berry (1999).
Mechanism of ubiquinol oxidation by the bc(1) complex: role of the iron sulfur protein and its mobility.
  Biochemistry, 38, 15791-15806.  
10468555 A.R.Crofts, S.Hong, N.Ugulava, B.Barquera, R.Gennis, M.Guergova-Kuras, and E.A.Berry (1999).
Pathways for proton release during ubihydroquinone oxidation by the bc(1) complex.
  Proc Natl Acad Sci U S A, 96, 10021-10026.  
9888813 B.Xia, J.D.Pikus, W.Xia, K.McClay, R.J.Steffan, Y.K.Chae, W.M.Westler, J.L.Markley, and B.G.Fox (1999).
Detection and classification of hyperfine-shifted 1H, 2H, and 15N resonances of the Rieske ferredoxin component of toluene 4-monooxygenase.
  Biochemistry, 38, 727-739.  
10082790 C.H.Snyder, E.Denke, and B.L.Trumpower (1999).
Aromatic amino acids in the Rieske iron-sulfur protein do not form an obligatory conduit for electron transfer from the iron-sulfur cluster to the heme of cytochrome c1 in the cytochrome bc1 complex.
  Biochim Biophys Acta, 1410, 237-247.  
10433117 C.de Vitry, and O.Vallon (1999).
Mutants of Chlamydomonas: tools to study thylakoid membrane structure, function and biogenesis.
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10092855 G.Montoya, K.te Kaat, S.Rodgers, W.Nitschke, and I.Sinning (1999).
The cytochrome bc1 complex from Rhodovulum sulfidophilum is a dimer with six quinones per monomer and an additional 6-kDa component.
  Eur J Biochem, 259, 709-718.  
9930988 M.M.Pereira, J.N.Carita, and M.Teixeira (1999).
Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: characterization of the iron-sulfur centers from the dehydrogenases and investigation of the high-potential iron-sulfur protein function by in vitro reconstitution of the respiratory chain.
  Biochemistry, 38, 1276-1283.  
10353811 M.P.Golinelli, N.H.Chmiel, and S.S.David (1999).
Site-directed mutagenesis of the cysteine ligands to the [4Fe-4S] cluster of Escherichia coli MutY.
  Biochemistry, 38, 6997-7007.  
10512801 S.Izrailev, A.R.Crofts, E.A.Berry, and K.Schulten (1999).
Steered molecular dynamics simulation of the Rieske subunit motion in the cytochrome bc(1) complex.
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10413471 V.Schünemann, A.X.Trautwein, J.Illerhaus, and W.Haehnel (1999).
Mössbauer and electron paramagnetic resonance studies of the cytochrome bf complex.
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Energy transduction function of the quinone reactions in cytochrome bc complexes.
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How far divergent evolution goes in proteins.
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Structure and function of the cytochrome bc1 complex of mitochondria and photosynthetic bacteria.
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Interactions between the cytochrome b, cytochrome c1, and Fe-S protein subunits at the ubihydroquinone oxidation site of the bc1 complex of Rhodobacter capsulatus.
  Biochemistry, 37, 8105-8114.  
9634695 B.Kauppi, K.Lee, E.Carredano, R.E.Parales, D.T.Gibson, H.Eklund, and S.Ramaswamy (1998).
Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase.
  Structure, 6, 571-586.
PDB code: 1ndo
9653134 H.Kim, D.Xia, C.A.Yu, J.Z.Xia, A.M.Kachurin, L.Zhang, L.Yu, and J.Deisenhofer (1998).
Inhibitor binding changes domain mobility in the iron-sulfur protein of the mitochondrial bc1 complex from bovine heart.
  Proc Natl Acad Sci U S A, 95, 8026-8033.  
  9658021 M.Brugna, D.Albouy, and W.Nitschke (1998).
Diversity of cytochrome bc complexes: example of the Rieske protein in green sulfur bacteria.
  J Bacteriol, 180, 3719-3723.  
9751716 M.Rousset, Y.Montet, B.Guigliarelli, N.Forget, M.Asso, P.Bertrand, J.C.Fontecilla-Camps, and E.C.Hatchikian (1998).
[3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis.
  Proc Natl Acad Sci U S A, 95, 11625-11630.
PDB code: 1frf
9860833 M.V.Ponamarev, and W.A.Cramer (1998).
Perturbation of the internal water chain in cytochrome f of oxygenic photosynthesis: loss of the concerted reduction of cytochromes f and b6.
  Biochemistry, 37, 17199-17208.  
9693742 T.Ohnishi, V.D.Sled, T.Yano, T.Yagi, D.S.Burbaev, and A.D.Vinogradov (1998).
Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain.
  Biochim Biophys Acta, 1365, 301-308.  
9693740 U.Brandt (1998).
The chemistry and mechanics of ubihydroquinone oxidation at center P (Qo) of the cytochrome bc1 complex.
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Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria.
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PDB code: 1qcr
9305958 G.Brasseur, V.Sled, U.Liebl, T.Ohnishi, and F.Daldal (1997).
The amino-terminal portion of the Rieske iron-sulfur protein contributes to the ubihydroquinone oxidation site catalysis of the Rhodobacter capsulatus bc1 complex.
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Function-directed mutagenesis of the cytochrome b6f complex in Chlamydomonas reinhardtii: involvement of the cd loop of cytochrome b6 in quinol binding to the Q(o) site.
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Copper A of cytochrome c oxidase, a novel, long-embattled, biological electron-transfer site.
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Assembly of a [2Fe-2S]2+ cluster in a molecular variant of Clostridium pasteurianum rubredoxin.
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Synchrotron radiation applications to macromolecular crystallography.
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Biogenesis of respiratory cytochromes in bacteria.
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Conserved nonliganding residues of the Rhodobacter capsulatus Rieske iron-sulfur protein of the bc1 complex are essential for protein structure, properties of the [2Fe-2S] cluster, and communication with the quinone pool.
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8994881 A.Volbeda, J.C.Fontecilla-Camps, and M.Frey (1996).
Novel metal sites in protein structures.
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Reconstitution of the 2Fe-2S center and g = 1.89 electron paramagnetic resonance signal into overproduced Nostoc sp. PCC 7906 Rieske protein.
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8931557 G.M.Soriano, M.V.Ponamarev, G.S.Tae, and W.A.Cramer (1996).
Effect of the interdomain basic region of cytochrome f on its redox reactions in vivo.
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Functional implications of the structure of the 'Rieske' iron-sulfur protein of bovine heart mitochondrial cytochrome bc1 complex.
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