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Contents |
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446 a.a.
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419 a.a.
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379 a.a.
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241 a.a.
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196 a.a.
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106 a.a.
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81 a.a.
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64 a.a.
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33 a.a.
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62 a.a.
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22 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Electron transport
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Title:
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Cytochrome bc1 complex from bovine
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Structure:
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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.
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Source:
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Bos taurus. Cattle. Organism_taxid: 9913. Organ: heart. Tissue: heart muscle. Organelle: mitochondrion. Cellular_location: mitochondrial inner membrane. Cellular_location: mitochondrial inner membrane
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Biol. unit:
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22mer (from
)
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Resolution:
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3.00Å
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R-factor:
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0.260
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R-free:
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0.320
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Authors:
|
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S.Iwata,J.W.Lee,K.Okada,J.K.Lee,M.Iwata,S.Ramaswamy,B.K.Jap
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Key ref:
|
 |
S.Iwata
et al.
(1998).
Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.
Science,
281,
64-71.
PubMed id:
DOI:
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Date:
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19-May-98
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Release date:
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13-Jan-99
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PROCHECK
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Headers
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References
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P31800
(QCR1_BOVIN) -
Cytochrome b-c1 complex subunit 1, mitochondrial
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|
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Seq: Struc:
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 |
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480 a.a.
446 a.a.
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 |
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|
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P23004
(QCR2_BOVIN) -
Cytochrome b-c1 complex subunit 2, mitochondrial
|
|
|
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Seq: Struc:
|
 |
 |
 |
453 a.a.
419 a.a.
|
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P00157
(CYB_BOVIN) -
Cytochrome b
|
|
|
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Seq: Struc:
|
 |
 |
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379 a.a.
379 a.a.
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|
 |
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P00125
(CY1_BOVIN) -
Cytochrome c1, heme protein, mitochondrial
|
|
|
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Seq: Struc:
|
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 |
 |
325 a.a.
241 a.a.
|
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|
 |
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|
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P13272
(UCRI_BOVIN) -
Cytochrome b-c1 complex subunit Rieske, mitochondrial
|
|
|
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Seq: Struc:
|
 |
 |
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274 a.a.
196 a.a.
|
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P00129
(QCR7_BOVIN) -
Cytochrome b-c1 complex subunit 7
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|
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Seq: Struc:
|
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 |
 |
111 a.a.
106 a.a.*
|
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|
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P13271
(QCR8_BOVIN) -
Cytochrome b-c1 complex subunit 8
|
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|
|
Seq: Struc:
|
 |
 |
 |
82 a.a.
81 a.a.
|
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|
 |
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|
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|
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P00126
(QCR6_BOVIN) -
Cytochrome b-c1 complex subunit 6, mitochondrial
|
|
|
|
Seq: Struc:
|
 |
 |
 |
91 a.a.
64 a.a.
|
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|
|
|
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|
 |
 |
|
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|
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P13272
(UCRI_BOVIN) -
Cytochrome b-c1 complex subunit Rieske, mitochondrial
|
|
|
|
Seq: Struc:
|
 |
 |
 |
274 a.a.
33 a.a.
|
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|
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Enzyme class:
|
 |
Chains E, I:
E.C.1.10.2.2
- Ubiquinol--cytochrome-c reductase.
|
|
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Reaction:
|
 |
QH2 + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H+
|
 |
 |
 |
 |
 |
QH(2)
|
+
|
2
×
ferricytochrome c
Bound ligand (Het Group name = )
matches with 63.00% similarity
|
=
|
Q
|
+
|
2
×
ferrocytochrome c
|
+
|
2
×
H(+)
|
|
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 |
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
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|
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|
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|
|
Gene Ontology (GO) functional annotation
|
|
|
|
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|
 |
 |
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|
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|
Cellular component
|
membrane
|
7 terms
|
 |
|
Biological process
|
oxidation-reduction process
|
14 terms
|
 |
|
Biochemical function
|
catalytic activity
|
11 terms
|
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| |
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| |
|
DOI no:
|
Science
281:64-71
(1998)
|
|
PubMed id:
|
|
|
|
|
| |
|
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.
|
|
|
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|
 |
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|
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 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
D.Ghezzi,
P.Arzuffi,
M.Zordan,
C.Da Re,
C.Lamperti,
C.Benna,
P.D'Adamo,
D.Diodato,
R.Costa,
C.Mariotti,
G.Uziel,
C.Smiderle,
and
M.Zeviani
(2011).
Mutations in TTC19 cause mitochondrial complex III deficiency and neurological impairment in humans and flies.
|
| |
Nat Genet, 43,
259-263.
|
 |
|
|
|
|
 |
I.Bertini,
G.Cavallaro,
and
A.Rosato
(2011).
Principles and patterns in the interaction between mono-heme cytochrome c and its partners in electron transfer processes.
|
| |
Metallomics, 3,
354-362.
|
 |
|
|
|
|
 |
B.D.Freudenthal,
L.Gakhar,
S.Ramaswamy,
and
M.T.Washington
(2010).
Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange.
|
| |
Nat Struct Mol Biol, 17,
479-484.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
E.A.Berry,
L.S.Huang,
D.W.Lee,
F.Daldal,
K.Nagai,
and
N.Minagawa
(2010).
Ascochlorin is a novel, specific inhibitor of the mitochondrial cytochrome bc1 complex.
|
| |
Biochim Biophys Acta, 1797,
360-370.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
G.Lenaz,
and
M.L.Genova
(2010).
Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject.
|
| |
Antioxid Redox Signal, 12,
961.
|
 |
|
|
|
|
 |
J.W.Ballard,
and
R.G.Melvin
(2010).
Linking the mitochondrial genotype to the organismal phenotype.
|
| |
Mol Ecol, 19,
1523-1539.
|
 |
|
|
|
|
 |
K.L.Hsueh,
W.M.Westler,
and
J.L.Markley
(2010).
NMR investigations of the Rieske protein from Thermus thermophilus support a coupled proton and electron transfer mechanism.
|
| |
J Am Chem Soc, 132,
7908-7918.
|
 |
|
|
|
|
 |
K.McLuskey,
A.W.Roszak,
Y.Zhu,
and
N.W.Isaacs
(2010).
Crystal structures of all-alpha type membrane proteins.
|
| |
Eur Biophys J, 39,
723-755.
|
 |
|
|
|
|
 |
K.R.Vinothkumar,
and
R.Henderson
(2010).
Structures of membrane proteins.
|
| |
Q Rev Biophys, 43,
65.
|
 |
|
|
|
|
 |
M.C.Gil Borlado,
D.Moreno Lastres,
M.Gonzalez Hoyuela,
M.Moran,
A.Blazquez,
R.Pello,
L.Marin Buera,
T.Gabaldon,
J.J.Garcia Peñas,
M.A.Martín,
J.Arenas,
and
C.Ugalde
(2010).
Impact of the mitochondrial genetic background in complex III deficiency.
|
| |
PLoS One, 5,
0.
|
 |
|
|
|
|
 |
M.Marí,
A.Colell,
A.Morales,
C.von Montfort,
C.Garcia-Ruiz,
and
J.C.Fernández-Checa
(2010).
Redox control of liver function in health and disease.
|
| |
Antioxid Redox Signal, 12,
1295-1331.
|
 |
|
|
|
|
 |
M.Morán,
L.Marín-Buera,
M.C.Gil-Borlado,
H.Rivera,
A.Blázquez,
S.Seneca,
M.Vázquez-López,
J.Arenas,
M.A.Martín,
and
C.Ugalde
(2010).
Cellular pathophysiological consequences of BCS1L mutations in mitochondrial complex III enzyme deficiency.
|
| |
Hum Mutat, 31,
930-941.
|
 |
|
|
|
|
 |
P.R.Rich,
and
A.Maréchal
(2010).
The mitochondrial respiratory chain.
|
| |
Essays Biochem, 47,
1.
|
 |
|
|
|
|
 |
T.Endo,
K.Yamano,
and
S.Kawano
(2010).
Structural basis for the disulfide relay system in the mitochondrial intermembrane space.
|
| |
Antioxid Redox Signal, 13,
1359-1373.
|
 |
|
|
|
|
 |
B.Liu,
A.K.Tewari,
L.Zhang,
K.B.Green-Church,
J.L.Zweier,
Y.R.Chen,
and
G.He
(2009).
Proteomic analysis of protein tyrosine nitration after ischemia reperfusion injury: mitochondria as the major target.
|
| |
Biochim Biophys Acta, 1794,
476-485.
|
 |
|
|
|
|
 |
D.Arnoult,
F.Soares,
I.Tattoli,
C.Castanier,
D.J.Philpott,
and
S.E.Girardin
(2009).
An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix.
|
| |
J Cell Sci, 122,
3161-3168.
|
 |
|
|
|
|
 |
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.
|
| |
J Phys Chem A, 113,
653-667.
|
 |
|
|
|
|
 |
F.Millett,
and
B.Durham
(2009).
Chapter 5 Use of ruthenium photooxidation techniques to study electron transfer in the cytochrome bc1 complex.
|
| |
Methods Enzymol, 456,
95.
|
 |
|
|
|
|
 |
G.Saab-Rincón,
and
B.Valderrama
(2009).
Protein engineering of redox-active enzymes.
|
| |
Antioxid Redox Signal, 11,
167-192.
|
 |
|
|
|
|
 |
H.B.Gray,
and
J.R.Winkler
(2009).
Electron Flow through Proteins.
|
| |
Chem Phys Lett, 483,
1-9.
|
 |
|
|
|
|
 |
J.L.Cape,
D.Aidasani,
D.M.Kramer,
and
M.K.Bowman
(2009).
Substrate redox potential controls superoxide production kinetics in the cytochrome bc complex.
|
| |
Biochemistry, 48,
10716-10723.
|
 |
|
|
|
|
 |
L.Aguilera-Aguirre,
A.Bacsi,
A.Saavedra-Molina,
A.Kurosky,
S.Sur,
and
I.Boldogh
(2009).
Mitochondrial dysfunction increases allergic airway inflammation.
|
| |
J Immunol, 183,
5379-5387.
|
 |
|
|
|
|
 |
L.Azevedo,
J.Carneiro,
B.van Asch,
A.Moleirinho,
F.Pereira,
and
A.Amorim
(2009).
Epistatic interactions modulate the evolution of mammalian mitochondrial respiratory complex components.
|
| |
BMC Genomics, 10,
266.
|
 |
|
|
|
|
 |
M.Freigassner,
H.Pichler,
and
A.Glieder
(2009).
wTuning microbial hosts for membrane protein production.
|
| |
Microb Cell Fact, 8,
69.
|
 |
|
|
|
|
 |
M.P.Murphy
(2009).
How mitochondria produce reactive oxygen species.
|
| |
Biochem J, 417,
1.
|
 |
|
|
|
|
 |
M.S.Albury,
C.Elliott,
and
A.L.Moore
(2009).
Towards a structural elucidation of the alternative oxidase in plants.
|
| |
Physiol Plant, 137,
316-327.
|
 |
|
|
|
|
 |
M.Sarewicz,
M.Dutka,
W.Froncisz,
and
A.Osyczka
(2009).
Magnetic interactions sense changes in distance between heme b(L) and the iron-sulfur cluster in cytochrome bc(1).
|
| |
Biochemistry, 48,
5708-5720.
|
 |
|
|
|
|
 |
O.Moiseeva,
V.Bourdeau,
A.Roux,
X.Deschênes-Simard,
and
G.Ferbeyre
(2009).
Mitochondrial dysfunction contributes to oncogene-induced senescence.
|
| |
Mol Cell Biol, 29,
4495-4507.
|
 |
|
|
|
|
 |
P.Van Nieuwenhuyse,
T.Van Leeuwen,
J.Khajehali,
B.Vanholme,
and
L.Tirry
(2009).
Mutations in the mitochondrial cytochrome b of Tetranychus urticae Koch (Acari: Tetranychidae) confer cross-resistance between bifenazate and acequinocyl.
|
| |
Pest Manag Sci, 65,
404-412.
|
 |
|
|
|
|
 |
V.Zara,
L.Conte,
and
B.L.Trumpower
(2009).
Evidence that the assembly of the yeast cytochrome bc1 complex involves the formation of a large core structure in the inner mitochondrial membrane.
|
| |
FEBS J, 276,
1900-1914.
|
 |
|
|
|
|
 |
Z.Jiang,
J.J.Michal,
J.Chen,
T.F.Daniels,
T.Kunej,
M.D.Garcia,
C.T.Gaskins,
J.R.Busboom,
L.J.Alexander,
R.W.Wright,
and
M.D.Macneil
(2009).
Discovery of novel genetic networks associated with 19 economically important traits in beef cattle.
|
| |
Int J Biol Sci, 5,
528-542.
|
 |
|
|
|
|
 |
A.P.Komarov,
O.W.Rokhlin,
C.A.Yu,
and
A.V.Gudkov
(2008).
Functional genetic screening reveals the role of mitochondrial cytochrome b as a mediator of FAS-induced apoptosis.
|
| |
Proc Natl Acad Sci U S A, 105,
14453-14458.
|
 |
|
|
|
|
 |
A.R.Crofts,
J.T.Holland,
D.Victoria,
D.R.Kolling,
S.A.Dikanov,
R.Gilbreth,
S.Lhee,
R.Kuras,
and
M.G.Kuras
(2008).
The Q-cycle reviewed: How well does a monomeric mechanism of the bc(1) complex account for the function of a dimeric complex?
|
| |
Biochim Biophys Acta, 1777,
1001-1019.
|
 |
|
|
|
|
 |
B.Gurung,
L.Yu,
and
C.A.Yu
(2008).
Stigmatellin induces reduction of iron-sulfur protein in the oxidized cytochrome bc1 complex.
|
| |
J Biol Chem, 283,
28087-28094.
|
 |
|
|
|
|
 |
D.Xia,
L.Esser,
M.Elberry,
F.Zhou,
L.Yu,
and
C.A.Yu
(2008).
The road to the crystal structure of the cytochrome bc (1) complex from the anoxigenic, photosynthetic bacterium Rhodobacter sphaeroides.
|
| |
J Bioenerg Biomembr, 40,
485-492.
|
 |
|
|
|
|
 |
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.
|
 |
|
|
|
|
 |
E.J.Lesnefsky,
and
C.L.Hoppel
(2008).
Cardiolipin as an oxidative target in cardiac mitochondria in the aged rat.
|
| |
Biochim Biophys Acta, 1777,
1020-1027.
|
 |
|
|
|
|
 |
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.
|
| |
J Biol Inorg Chem, 13,
1301-1313.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
F.A.Rotsaert,
M.G.Ding,
and
B.L.Trumpower
(2008).
Differential efficacy of inhibition of mitochondrial and bacterial cytochrome bc1 complexes by center N inhibitors antimycin, ilicicolin H and funiculosin.
|
| |
Biochim Biophys Acta, 1777,
211-219.
|
 |
|
|
|
|
 |
H.Sumimoto
(2008).
Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species.
|
| |
FEBS J, 275,
3249-3277.
|
 |
|
|
|
|
 |
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.
|
| |
Biochim Biophys Acta, 1777,
317-326.
|
 |
|
|
|
|
 |
J.I.Yeh,
U.Chinte,
and
S.Du
(2008).
Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism.
|
| |
Proc Natl Acad Sci U S A, 105,
3280-3285.
|
 |
|
PDB codes:
|
 |
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