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Electron transport PDB-id
1be3
Asymmetric unit
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Contents
Description
Header details
Header records
References
PROCHECK
Protein chains
446 a.a. *
419 a.a. *
379 a.a. *
241 a.a. *
196 a.a. *
106 a.a. *
81 a.a. *
64 a.a. *
33 a.a. *
62 a.a. *
22 a.a. *
Ligands
HEM ×2
HEC
FES

* Residue conservation analysis
Tools
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Clefts Calculation
  
  Biological unit*, 22mer
(*as deduced by PQS)
PDB id: 1be3
Name: Electron transport
Title: Cytochrome bc1 complex from bovine

Structure:
Cytochrome bc1 complex. Chain: a. Synonym: ubiquinol cytochromE C oxidoreductase, complex iii. Cytochrome bc1 complex. Chain: b. Synonym: ubiquinol cytochromE C oxidoreductase, complex iii. Cytochrome bc1 complex.

Source:
Bos taurus. Cattle. Organism_taxid: 9913. Organ: heart. Tissue: heart muscle. Organelle: mitochondrion. Cellular_location: mitochondrial inner membrane. Cellular_location: mitochondrial inner membrane

Biological unit:
22mer (from PQS)

UniProt:
Chain A: P31800 (QCR1_BOVIN)
Pfam  
Seq:
Struc:
Seq: 480 a.a.
Struc: 446 a.a.

Chain B: P23004 (QCR2_BOVIN)
Pfam  
Seq:
Struc:
Seq: 453 a.a.
Struc: 419 a.a.

Chain C: P00157 (CYB_BOVIN)
Pfam  
Seq:
Struc:
Seq: 379 a.a.
Struc: 379 a.a.

Chain D: P00125 (CY1_BOVIN)
Pfam  
Seq:
Struc:
Seq: 325 a.a.
Struc: 241 a.a.

Chain E: P13272 (UCRI_BOVIN)
Pfam  
Seq:
Struc:
Seq: 274 a.a.
Struc: 196 a.a.

Chain F: P00129 (QCR7_BOVIN)
Pfam  
Seq: 111 a.a.
Struc: 106 a.a.*

Chain G: P13271 (QCR8_BOVIN)
Pfam  
Seq: 82 a.a.
Struc: 81 a.a.

Chain H: P00126 (QCR6_BOVIN)
Pfam  
Seq: 91 a.a.
Struc: 64 a.a.

Chain I: P13272 (UCRI_BOVIN)
Pfam  
Seq:
Struc:
Seq: 274 a.a.
Struc: 33 a.a.

Chain J: P00130 (QCR9_BOVIN)
Pfam  
Seq: 64 a.a.
Struc: 62 a.a.

Chain K: P07552 (QCR10_BOVIN)
Pfam  
Seq: 56 a.a.
Struc: 22 a.a.*
Key:    PfamA domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme class:
Chains E, I: E.C.1.10.2.2   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:
QH2 + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H+ (see diagram below)

Resolution:
3.00Å

R-factor:
0.260

R-free:
0.320

Authors:
S.Iwata,J.W.Lee,K.Okada,J.K.Lee,M.Iwata,S.Ramaswamy,B.K.Jap

Key ref:
S.Iwata et al. (1998). Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.. Science, 281, 64-71. [PubMed id: 9651245] [DOI: 10.1126/science.281.5373.64]

Date:
19-May-98

Release date:
13-Jan-99
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Enzyme reaction for E.C.1.10.2.2


QH(2)
+
2 × ferricytochrome c
=
Q
+

2 × ferrocytochrome c
Bound ligand (Het Group name = HEM)
matches with 70.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

 
    Key reference    
 
 
DOI no: 10.1126/science.281.5373.64 Science 281:64-71 (1998)
PubMed id: 9651245  
 
 
Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.
S.Iwata, J.W.Lee, K.Okada, J.K.Lee, M.Iwata, B.Rasmussen, T.A.Link, S.Ramaswamy, B.K.Jap.
 
  ABSTRACT  
 
Mitochondrial cytochrome bc1 complex performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial targeting presequence. Refined crystal structures of the 11-subunit bc1 complex from bovine heart reveal full views of this bifunctional enzyme. The "Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new electron transport mechanism of the enzyme. The mitochondrial targeting presequence of the "Rieske" protein (subunit 9) is lodged between the two "core" subunits at the matrix side of the complex. These "core" subunits are related to the matrix processing peptidase, and the structure unveils how mitochondrial targeting presequences are recognized.
 
  Selected figure(s)  
 
Figure 3.
Fig. 3. Interaction of the mitochondrial targeting presequence of the ISP (subunit 9 in bright red) with the two core subunits (core^ 1 in aqua blue and core 2 in green). (A) Position of subunit 9 between the core 1 and core 2 subunits viewed from the mitochondrial matrix side of the complex. The cleaved NH[2]-terminal arm of the^ ISP is shown in magenta. The -sheet of the NH[2]-terminal domain of core 2 is highlighted (yellowish green), and the two possible^ Zn2+-binding sites are marked by black arrowheads. (B) Stereoview of various interactions between the COOH-terminal -strand of^ subunit 9 and its binding site in the core 2 subunit.
Figure 4.
Fig. 4. Structural comparison of the ISP in P6[5]22 and P6[5] crystal forms of bovine cytochrome bc[1]. Stereoview of the superimposed ISP functional domains at "c[1]" (red) and "Int" (blue) positional states using the base folds. The cluster-binding folds are shown in saturated^ colors, whereas the base folds are shown in pale colors. These^ structures are related by a hinge motion and the isomerization of Pro175 near the [2Fe-2S] center.
 
  The above figures are reprinted by permission from the AAAs: Science (1998, 281, 64-71) copyright 1998.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

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19236481 V.Zara, L.Conte, and B.L.Trumpower (2009).
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PDB code: 2qpz
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Metals in membranes.
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Redox pathways of the mitochondrion.
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Deleterious epistatic interactions between electron transport system protein-coding loci in the copepod Tigriopus californicus.
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  FEBS J, 273, 4817-4830.  
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  Proc Natl Acad Sci U S A, 103, 16212-16217.
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Gene expression analysis exposes mitochondrial abnormalities in a mouse model of Rett syndrome.
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Transmembrane traffic in the cytochrome b6f complex.
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Role of glycosylation and membrane environment in nicotinic acetylcholine receptor stability.
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The single chlorophyll a molecule in the cytochrome b6f complex: unusual optical properties protect the complex against singlet oxygen.
  Biophys J, 88, 4178-4187.  
15713802 N.V.Dudkina, H.Eubel, W.Keegstra, E.J.Boekema, and H.P.Braun (2005).
Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III.
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Multiple Rieske genes in prokaryotes: exchangeable Rieske subunits in the cytochrome bc-complex of Rubrivivax gelatinosus.
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Reversible redox energy coupling in electron transfer chains.
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The cytochrome bc1 complex: function in the context of structure.
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Mitochondrial cytochrome c1 is a collapsed di-heme cytochrome.
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Ageing, oxidative stress, and mitochondrial uncoupling.
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The complex architecture of oxygenic photosynthesis.
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Structural genomics of membrane proteins.
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Crystallization and preliminary X-ray diffraction studies of the hyperthermophilic archaeal sulredoxin having the unique Rieske [2Fe-2S] cluster environment.
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Further insights into the assembly of the yeast cytochrome bc1 complex based on analysis of single and double deletion mutants lacking supernumerary subunits and cytochrome b.
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Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism.
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Hydrophobicity of transmembrane proteins: spatially profiling the distribution.
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An atypical haem in the cytochrome b(6)f complex.
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PDB code: 1q90
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Biosynthesis and biophysical analysis of domains of a yeast G protein-coupled receptor.
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Redox regulation of thylakoid protein phosphorylation.
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Crystal structure of the bromide-bound D85S mutant of bacteriorhodopsin: principles of ion pumping.
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PDB code: 1mgy
12595738 R.Horsefield, V.Yankovskaya, S.Törnroth, C.Luna-Chavez, E.Stambouli, J.Barber, B.Byrne, G.Cecchini, and S.Iwata (2003).
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"Ping-pong" interactions between mitochondrial tRNA import receptors within a multiprotein complex.
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Oils used in microbatch crystallization do not remove a detergent from the drops they cover.
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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
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.  
11880631 C.Lange, and C.Hunte (2002).
Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c.
  Proc Natl Acad Sci U S A, 99, 2800-2805.
PDB code: 1kyo
12441376 C.P.Chen, and B.Rost (2002).
Long membrane helices and short loops predicted less accurately.
  Protein Sci, 11, 2766-2773.  
12044181 G.Finazzi (2002).
Redox-coupled proton pumping activity in cytochrome b6f, as evidenced by the pH dependence of electron transfer in whole cells of Chlamydomonas reinhardtii.
  Biochemistry, 41, 7475-7482.  
  18629259 I.Mus-Veteau (2002).
Heterologous expression and purification systems for structural proteomics of Mammalian membrane proteins.
  Comp Funct Genomics, 3, 511-517.  
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.  
11967568 M.J.Maté, M.Ortiz-Lombardía, B.Boitel, A.Haouz, D.Tello, S.A.Susin, J.Penninger, G.Kroemer, and P.M.Alzari (2002).
The crystal structure of the mouse apoptosis-inducing factor AIF.
  Nat Struct Biol, 9, 442-446.
PDB code: 1gv4
12391595 M.Tanaka, N.Fuku, T.Takeyasu, L.J.Guo, R.Hirose, M.Kurata, H.J.Borgeld, Y.Yamada, W.Maruyama, Y.Arai, N.Hirose, Y.Oshida, Y.Sato, N.Hattori, Y.Mizuno, S.Iwata, and K.Yagi (2002).
Golden mean to longevity: rareness of mitochondrial cytochrome b variants in centenarians but not in patients with Parkinson's disease.
  J Neurosci Res, 70, 347-355.  
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.  
11916874 S.Georgakopoulou, R.N.Frese, E.Johnson, C.Koolhaas, R.J.Cogdell, R.van Grondelle, and G.van der Zwan (2002).
Absorption and CD spectroscopy and modeling of various LH2 complexes from purple bacteria.
  Biophys J, 82, 2184-2197.  
12081951 S.Ouchane, I.Agalidis, and C.Astier (2002).
Natural resistance to inhibitors of the ubiquinol cytochrome c oxidoreductase of Rubrivivax gelatinosus: sequence and functional analysis of the cytochrome bc(1) complex.
  J Bacteriol, 184, 3815-3822.  
11331012 A.M.Grosset, B.R.Gibney, F.Rabanal, C.C.Moser, and P.L.Dutton (2001).
Proof of principle in a de novo designed protein maquette: an allosterically regulated, charge-activated conformational switch in a tetra-alpha-helix bundle.
  Biochemistry, 40, 5474-5487.  
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.  
11726495 C.Lange, J.H.Nett, B.L.Trumpower, and C.Hunte (2001).
Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure.
  EMBO J, 20, 6591-6600.
PDB code: 1kb9
11447103 F.A.Wollman (2001).
State transitions reveal the dynamics and flexibility of the photosynthetic apparatus.
  EMBO J, 20, 3623-3630.  
11226222 F.Cutruzzola, K.Brown, E.K.Wilson, A.Bellelli, M.Arese, M.Tegoni, C.Cambillau, and M.Brunori (2001).
The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties.
  Proc Natl Acad Sci U S A, 98, 2232-2237.  
11601507 F.Wibrand, K.Ravn, M.Schwartz, T.Rosenberg, N.Horn, and J.Vissing (2001).
Multisystem disorder associated with a missense mutation in the mitochondrial cytochrome b gene.
  Ann Neurol, 50, 540-543.  
11735976 J.A.Tuszyński, and J.M.Dixon (2001).
Quantitative analysis of the frequency spectrum of the radiation emitted by cytochrome oxidase enzymes.
  Phys Rev E Stat Nonlin Soft Matter Phys, 64, 051915.  
11329288 J.E.McLean, E.A.Neidhardt, T.H.Grossman, and L.Hedstrom (2001).
Multiple inhibitor analysis of the brequinar and leflunomide binding sites on human dihydroorotate dehydrogenase.
  Biochemistry, 40, 2194-2200.  
11148026 M.Ghosh, Y.Wang, C.E.Ebert, S.Vadlamuri, and D.S.Beattie (2001).
Substituting leucine for alanine-86 in the tether region of the iron-sulfur protein of the cytochrome bc1 complex affects the mobility of the [2Fe2S] domain.
  Biochemistry, 40, 327-335.  
11722564 R.Covián, and R.Moreno-Sánchez (2001).
Role of protonatable groups of bovine heart bc(1) complex in ubiquinol binding and oxidation.
  Eur J Biochem, 268, 5783-5790.  
11425236 S.Quaranta, M.G.Giuffrida, M.Cavaletto, C.Giunta, J.Godovac-Zimmermann, B.Cañas, C.Fabris, E.Bertino, M.Mombrò, and A.Conti (2001).
Human proteome enhancement: high-recovery method and improved two-dimensional map of colostral fat globule membrane proteins.
  Electrophoresis, 22, 1810-1818.  
11576427 X.P.Zhang, S.Sjöling, M.Tanudji, L.Somogyi, D.Andreu, L.E.Eriksson, A.Gräslund, J.Whelan, and E.Glaser (2001).
Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase.
  Plant J, 27, 427-438.  
11722777 Y.Munekage, S.Takeda, T.Endo, P.Jahns, T.Hashimoto, and T.Shikanai (2001).
Cytochrome b(6)f mutation specifically affects thermal dissipation of absorbed light energy in Arabidopsis.
  Plant J, 28, 351-359.  
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.  
10960495 A.L.Andreu, N.Checcarelli, S.Iwata, S.Shanske, and S.DiMauro (2000).
A missense mutation in the mitochondrial cytochrome b gene in a revisited case with histiocytoid cardiomyopathy.
  Pediatr Res, 48, 311-314.  
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.  
10632712 C.Schwarze, A.V.Carluccio, G.Venturoli, and A.Labahn (2000).
Photo-induced cyclic electron transfer involving cytochrome bc1 complex and reaction center in the obligate aerobic phototroph Roseobacter denitrificans.
  Eur J Biochem, 267, 422-433.  
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.  
10781061 E.Darrouzet, M.Valkova-Valchanova, C.C.Moser, P.L.Dutton, and F.Daldal (2000).
Uncovering the [2Fe2S] domain movement in cytochrome bc1 and its implications for energy conversion.
  Proc Natl Acad Sci U S A, 97, 4567-4572.  
11112533 E.Darrouzet, M.Valkova-Valchanova, and F.Daldal (2000).
Probing the role of the Fe-S subunit hinge region during Q(o) site catalysis in Rhodobacter capsulatus bc(1) complex.
  Biochemistry, 39, 15475-15483.  
10809709 G.Zheng, R.Hehn, and P.Zuber (2000).
Mutational analysis of the sbo-alb locus of Bacillus subtilis: identification of genes required for subtilosin production and immunity.
  J Bacteriol, 182, 3266-3273.  
11047755 J.A.Keightley, R.Anitori, M.D.Burton, F.Quan, N.R.Buist, and N.G.Kennaway (2000).
Mitochondrial encephalomyopathy and complex III deficiency associated with a stop-codon mutation in the cytochrome b gene.
  Am J Hum Genet, 67, 1400-1410.  
10944359 J.Abramson, G.Larsson, B.Byrne, A.Puustinen, A.Garcia-Horsman, and S.Iwata (2000).
Purification, crystallization and preliminary crystallographic studies of an integral membrane protein, cytochrome bo3 ubiquinol oxidase from Escherichia coli.
  Acta Crystallogr D Biol Crystallogr, 56, 1076-1078.  
10971589 J.H.Nett, C.Hunte, and B.L.Trumpower (2000).
Changes to the length of the flexible linker region of the Rieske protein impair the interaction of ubiquinol with the cytochrome bc1 complex.
  Eur J Biochem, 267, 5777-5782.  
10966478 J.L.Popot, and D.M.Engelman (2000).
Helical membrane protein folding, stability, and evolution.
  Annu Rev Biochem, 69, 881-922.  
11101297 J.M.Shifman, B.R.Gibney, R.E.Sharp, and P.L.Dutton (2000).
Heme redox potential control in de novo designed four-alpha-helix bundle proteins.
  Biochemistry, 39, 14813-14821.  
11112550 K.Kobayashi, S.Tagawa, and T.Mogi (2000).
Transient formation of ubisemiquinone radical and subsequent electron transfer process in the Escherichia coli cytochrome bo.
  Biochemistry, 39, 15620-15625.  
10852722 L.A.Sazanov, S.Y.Peak-Chew, I.M.Fearnley, and J.E.Walker (2000).
Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme.
  Biochemistry, 39, 7229-7235.  
10681446 M.Brugna, S.Rodgers, A.Schricker, G.Montoya, M.Kazmeier, W.Nitschke, and I.Sinning (2000).
A spectroscopic method for observing the domain movement of the Rieske iron-sulfur protein.
  Proc Natl Acad Sci U S A, 97, 2069-2074.  
10823938 M.Eilers, S.C.Shekar, T.Shieh, S.O.Smith, and P.J.Fleming (2000).
Internal packing of helical membrane proteins.
  Proc Natl Acad Sci U S A, 97, 5796-5801.  
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.  
10898682 M.Korsinczky, N.Chen, B.Kotecka, A.Saul, K.Rieckmann, and Q.Cheng (2000).
Mutations in Plasmodium falciparum cytochrome b that are associated with atovaquone resistance are located at a putative drug-binding site.
  Antimicrob Agents Chemother, 44, 2100-2108.  
11079541 M.Rana, I.de Coo, F.Diaz, H.Smeets, and C.T.Moraes (2000).
An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production.
  Ann Neurol, 48, 774-781.  
11112534 M.Valkova-Valchanova, E.Darrouzet, C.R.Moomaw, C.A.Slaughter, and F.Daldal (2000).
Proteolytic cleavage of the Fe-S subunit hinge region of Rhodobacter capsulatus bc(1) complex: effects of inhibitors and mutations.
  Biochemistry, 39, 15484-15492.  
10704472 M.van Geest, and J.S.Lolkema (2000).
Membrane topology and insertion of membrane proteins: search for topogenic signals.
  Microbiol Mol Biol Rev, 64, 13-33.  
11123802 P.Dessi, C.Rudhe, and E.Glaser (2000).
Studies on the topology of the protein import channel in relation to the plant mitochondrial processing peptidase integrated into the cytochrome bc1 complex.
  Plant J, 24, 637-644.  
10757970 R.C.Sadoski, G.Engstrom, H.Tian, L.Zhang, C.A.Yu, L.Yu, B.Durham, and F.Millett (2000).
Use of a photoactivated ruthenium dimer complex to measure electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the cytochrome bc(1) complex.
  Biochemistry, 39, 4231-4236.  
10704220 S.Heimann, M.V.Ponamarev, and W.A.Cramer (2000).
Movement of the Rieske iron-sulfur protein in the p-side bulk aqueous phase: effect of lumenal viscosity on redox reactions of the cytochrome b6f complex.
  Biochemistry, 39, 2692-2699.  
10848994 S.Rodgers, C.Moser, M.Martinez-Julvez, and I.Sinning (2000).
Deletion of the 6-kDa subunit affects the activity and yield of the bc1 complex from Rhodovulum sulfidophilum.
  Eur J Biochem, 267, 3753-3761.  
11112521 T.C.Mueser, P.H.Rogers, and A.Arnone (2000).
Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin.
  Biochemistry, 39, 15353-15364.
PDB codes: 1g08 1g09 1g0a 1g0b
11123950 V.P.Shinkarev, N.B.Ugulava, A.R.Crofts, and C.A.Wraight (2000).
DCCD inhibits the reactions of the iron-sulfur protein in Rhodobacter sphaeroides chromatophores.
  Biochemistry, 39, 16206-16212.  
11087372 V.P.Shinkarev, N.B.Ugulava, E.Takahashi, A.R.Crofts, and C.A.Wraight (2000).
Aspartate-187 of cytochrome b is not needed for DCCD inhibition of ubiquinol: cytochrome c oxidoreductase in Rhodobacter sphaeroides chromatophores.
  Biochemistry, 39, 14232-14237.  
10786880 V.Santoni, M.Molloy, and T.Rabilloud (2000).
Membrane proteins and proteomics: un amour impossible?
  Electrophoresis, 21, 1054-1070.  
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.  
10625447 A.R.Crofts, S.Hong, Z.Zhang, and E.A.Berry (1999).
Physicochemical aspects of the movement of the rieske iron sulfur protein during quinol oxidation by the bc(1) complex from mitochondria and photosynthetic bacteria.
  Biochemistry, 38, 15827-15839.  
  10464208 A.S.Saribas, S.Mandaci, and F.Daldal (1999).
An engineered cytochrome b6c1 complex with a split cytochrome b is able to support photosynthetic growth of Rhodobacter capsulatus.
  J Bacteriol, 181, 5365-5372.  
10413476 B.Gomez, and N.C.Robinson (1999).
Phospholipase digestion of bound cardiolipin reversibly inactivates bovine cytochrome bc1.
  Biochemistry, 38, 9031-9038.  
  10416021 C.A.Yu, L.Zhang, K.P.Deng, H.Tian, D.Xia, H.Kim, J.Deisenhofer, and L.Yu (1999).
Structure and reaction mechanisms of multifunctional mitochondrial cytochrome bc1 complex.
  Biofactors, 9, 103-109.  
10508156 C.M.Cruciat, K.Hell, H.Fölsch, W.Neupert, and R.A.Stuart (1999).
Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc(1) complex.
  EMBO J, 18, 5226-5233.  
10387032 E.Darrouzet, S.Mandaci, J.Li, H.Qin, D.B.Knaff, and F.Daldal (1999).
Substitution of the sixth axial ligand of Rhodobacter capsulatus cytochrome c1 heme yields novel cytochrome c1 variants with unusual properties.
  Biochemistry, 38, 7908-7917.  
10357809 F.Zito, G.Finazzi, R.Delosme, W.Nitschke, D.Picot, and F.A.Wollman (1999).
The Qo site of cytochrome b6f complexes controls the activation of the LHCII kinase.
  EMBO J, 18, 2961-2969.  
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.  
  10572140 G.Zheng, L.Z.Yan, J.C.Vederas, and P.Zuber (1999).
Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin.
  J Bacteriol, 181, 7346-7355.  
10447880 I.K.Srivastava, J.M.Morrisey, E.Darrouzet, F.Daldal, and A.B.Vaidya (1999).
Resistance mutations reveal the atovaquone-binding domain of cytochrome b in malaria parasites.
  Mol Microbiol, 33, 704-711.  
10611277 K.E.McAuley, P.K.Fyfe, J.P.Ridge, N.W.Isaacs, R.J.Cogdell, and M.R.Jones (1999).
Structural details of an interaction between cardiolipin and an integral membrane protein.
  Proc Natl Acad Sci U S A, 96, 14706-14711.
PDB code: 1qov
  10595562 K.S.Makarova, and N.V.Grishin (1999).
Thermolysin and mitochondrial processing peptidase: how far structure-functional convergence goes.
  Protein Sci, 8, 2537-2540.  
10531513 P.F.Lindley (1999).
Macromolecular crystallography with a third-generation synchrotron source.
  Acta Crystallogr D Biol Crystallogr, 55, 1654-1662.  
10079091 R.E.Sharp, A.Palmitessa, B.R.Gibney, J.L.White, C.C.Moser, F.Daldal, and P.L.Dutton (1999).
Ubiquinone binding capacity of the Rhodobacter capsulatus cytochrome bc1 complex: effect of diphenylamine, a weak binding QO site inhibitor.
  Biochemistry, 38, 3440-3446.  
10555979 R.E.Sharp, B.R.Gibney, A.Palmitessa, J.L.White, J.A.Dixon, C.C.Moser, F.Daldal, and P.L.Dutton (1999).
Effect of inhibitors on the ubiquinone binding capacity of the primary energy conversion site in the Rhodobacter capsulatus cytochrome bc(1) complex.
  Biochemistry, 38, 14973-14980.  
10410805 S.H.White, and W.C.Wimley (1999).
Membrane protein folding and stability: physical principles.
  Annu Rev Biophys Biomol Struct, 28, 319-365.  
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.
  Biophys J, 77, 1753-1768.  
  10416020 U.Brandt (1999).
Proton translocation in the respiratory chain involving ubiquinone--a hypothetical semiquinone switch mechanism for complex I.
  Biofactors, 9, 95.  
10413471 V.Schünemann, A.X.Trautwein, J.Illerhaus, and W.Haehnel (1999).
Mössbauer and electron paramagnetic resonance studies of the cytochrome bf complex.
  Biochemistry, 38, 8981-8991.  
  10416018 W.A.Cramer, and G.M.Soriano (1999).
Energy transduction function of the quinone reactions in cytochrome bc complexes.
  Biofactors, 9, 81-86.  
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.  
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