Structural studies of cytochrome b5 and cytochrome
b5-like domains
By Kirill Degtyarenko
Last modified: Wed Apr 14 12:24:06 BST 2004
-
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Identification by proton nuclear magnetic resonance of the histidines in
cytochrome b5 modified by diethyl pyrocarbonate.
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The structure of ferrocytochrome b5 at 2.8 Å
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The solution structure of oxidized rat microsomal cytochrome
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-
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Solution structure of oxidized rat microsomal cytochrome b5
in the presence of 2 M guanidinium chloride: Monitoring the early steps in
protein unfolding.
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Solution structure of the B form of oxidized rat microsomal cytochrome
b5 and backbone dynamics via 15N
rotating-frame NMR-relaxation measurements.
Biological implications.
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Monitoring mobility in the early steps of unfolding: the case of oxidized
cytochrome b5 in the presence of 2 M guanidinium chloride.
Biochemistry 39, 7117-7130.
[Supplementary Material]
- Avila, L., Huang, H.-w., Rodríguez, J.C., Moënne-Loccoz, P. and
Rivera, M. (2000)
Oxygen activation by axial ligand mutants of mitochondrial cytochrome
b5: Oxidation of heme to verdoheme and biliverdin.
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[Supplementary Material]
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Solution structure of reduced microsomal rat cytochrome b5.
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Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome
b5 via 15N rotating frame NMR relaxation
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Biochemistry 37, 12320-12330.
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Partial orientation of oxidized and reduced cytochrome b5 at
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15N chemical shift changes in cytochrome b5:
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[published erratum
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Surface differences and similarities in two homologous proteins. Cytochrome
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Structural studies of cytochrome b5:
Complete sequence-specific resonance assignments for the
trypsin-solubilized microsomal ferrocytochrome b5
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Sequence-specific 1H and 15N resonance assignments
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Guiles, R.D., Basus, V.J., Sarma, S., Malpure, S., Fox, K.M., Kuntz, I.D. and
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Novel heteronuclear methods of assignment transfer from a diamagnetic to
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Guiles, R.D., Sarma, S., DiGate, R.J., Banville, D., Basus, V.J., Kuntz, I.D.
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Pseudocontact shifts used in the restraint of the solution structures of
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In vitro membrane-inserted conformation of the cytochrome
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NMR study of the interaction between cytochrome b5 and
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Hewson, R., Newbold, R.J. and Whitford, D. (1993)
The expression of bovine microsomal cytochrome b5 in
Escherichia coli and a study of the solution structure and stability of
variant proteins.
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Hom, K., Ma, Q.-F., Wolfe, G., Zhang, H., Storch, E.M., Daggett, V.,
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NMR studies of the association of cytochrome b5 with
cytochrome c.
Biochemistry 39, 14025-14039.
[Supplementary Material]
-
Hori, A., Hayashi, F., Kyogoku, Y. and Akutsu, H. (1988)
A photo-chemically induced dynamic nuclear polarization NMR study on
rabbit and bovine cytochrome b5.
Eur. J. Biochem. 174, 503-508.
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Hunter, C.L., Lloyd, E., Eltis, L.D., Rafferty, S.P., Lee, H., Smith, M. and
Mauk, A.G. (1997)
Role of the heme propionates in the interaction of heme with apomyoglobin
and apocytochrome b5.
Biochemistry 36, 1010-1017.
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Ihara, M., Takahashi, S., Ishimori, K. and Morishima, I. (2000)
Functions of fluctuation in the heme-binding loops of cytochrome
b5 revealed in the process of heme incorporation.
Biochemistry 39, 5961-5970.
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Keller, R.M. and Wüthrich, K. (1980)
Structural study of the heme crevice in cytochrome b5 based
on individual assignments of the 1H-NMR lines of the heme group
and selected amino acid residues.
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Keller, R.M., Groudinsky, O. and Wüthrich, K. (1976)
Contact-shifted resonances in the 1H NMR spectra of cytochrome
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the heme group.
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Kelly, G.P., Muskett, F.W. and Whitford, D. (1997)
Analysis of backbone dynamics in cytochrome b5 using
15N-NMR relaxation measurements.
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Structure and characterization of Ectothiorhodospira vacuolata
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Labeyrie, F., Beloeil, J.C. and Thomas, M.A. (1988)
Evidence by NMR for mobility of the cytochrome domain within flavocytochrome
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1H NMR study of the influence of hydrophobic contacts on
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Lee, K.B., La Mar, G.N., Pandey, R.K., Rezzano, I.N., Mansfield, K.E. and
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1H NMR study of the role of heme carboxylate side chains in
modulating heme pocket structure and the mechanism of reconstitution
of cytochrome b5.
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Interpretation of hyperfine shift patterns in ferricytochromes
b5 in terms of angular position of the heme: a sensitive
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Hydrogen isotope effects on the proton nuclear magnetic resonance spectrum of
bovine ferricytochrome b5: Axial hydrogen bonding involving
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Myoglobin:cytochrome b5 interactions and the kinetic
mechanism of metmyoglobin reductase.
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Recombinant human erythrocyte cytochrome b5.
Biochemistry 33, 11432-11437.
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1H-NMR assignments and the dynamics of interconversion of the
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Manyusa, S. and Whitford, D. (1999)
Defining folding and unfolding reactions of apocytochrome b5
using equilibrium and kinetic fluorescence measurements.
Biochemistry 38, 9533-9540.
-
Manyusa, S., Mortuza, G.B. and Whitford, D. (1999)
Analysis of folding and unfolding reactions of cytochrome b5.
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[Supplementary Material]
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Mathews, F.S. (1980)
The orientation of the heme group in crystalline cytochrome
b5.
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Mathews, F.S., Argos, P. and Levine, M. (1972)
The structure of cytochrome b5 at 2.0 Angstrom resolution.
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Moore, C.D. and Lecomte, J.T.J. (1990)
Structural properties of apocytochrome b5: presence of
a stable native core.
Biochemistry 29, 1984-1989.
-
Moore, C.D. and Lecomte, J.T.J. (1993)
Characterization of an independent structural unit in apocytochrome
b5.
Biochemistry 32, 199-207.
-
Moore, C.D., al-Misky, O.N. and Lecomte, J.T.J. (1991)
Similarities in structure between holocytochrome b5 and
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Biochemistry 30, 8357-8365.
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Mortuza, G.B. and Whitford, D. (1997)
Mutagenesis of residues 27 and 78 modulates heme orientation in cytochrome
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Kinetic and crystallographic studies on the active site Arg289Lys mutant of
flavocytochrome b2 (yeast L-lactate
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Biochemistry 39, 3266-3275.
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Muskett, F.W., Kelly, G.P. and Whitford, D. (1996)
The solution structure of bovine ferricytochrome b5
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Qian, W., Sun, Y.-L., Wang, Y.-H., Zhuang, J.-H., Xie, Y.
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The influence of mutation at Glu44 and Glu56 of cytochrome b5
on the protein's stabilization and interaction between cytochrome c
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Biochemistry 37, 14137-14150.
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Kinetic studies of electron transfer in the cyt
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Electron transfer from cytochrome b5 to iron and copper
complexes.
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Rivera, M., Barillas-Mury, C., Christensen, K.A., Little, J.W.,
Wells, M.A. and Walker, F.A. (1992)
Gene synthesis, bacterial expression, and 1H NMR spectroscopic
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Biochemistry 31, 12233-12240.
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Rivera, M., Wells, M.A. and Walker, F.A. (1994)
Cation-promoted cyclic voltammetry of recombinant rat outer mitochondrial
membrane cytochrome b5 at a gold electrode modified with
-mercaptopropionic
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Biochemistry 33, 2161-2170.
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Rivera, M., Seetharaman, R., Girdhar, D., Wirtz, M., Zhang, X., Wang, X. and
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The reduction potential of cytochrome b5 is modulated by its
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Biochemistry 37, 1485-1494.
-
Rivera, M., Qiu, F., Bunce, R.A. and Stark, R.E. (1999)
Complete isomer-specific 1H and 13C NMR
assignments of the heme resonances of rat liver outer mitochondrial membrane
cytochrome b5.
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Conversion of mitochondrial cytochrome b5 into a species
capable of performing the efficient coupled oxidation of heme.
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13C NMR spectroscopic and X-ray crystallographic study of the
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A comparison of the heme binding pocket in globins and cytochrome
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1H, 13C and 15N NMR assignments and secondary
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Characterization of a site-directed mutant of cytochrome
b5 designed to alter axial imidazole ligand plane
orientation.
Biochemistry 36, 5645-5657.
-
Sarma, S., DiGate, R.J., Goodin, D.B., Miller, C.J. and Guiles, R.D.
(1997b)
Effect of axial ligand plane reorientation on electronic and electrochemical
properties observed in the A67V mutant of rat cytochrome b5.
Biochemistry 36, 5658-5668.
-
Storch, E.M., Daggett, V. and Atkins, W.A. (1999a)
Engineering out motion: Introduction of a de novo disulfide bond and a
salt bridge designed to close a dynamic cleft on the surface of cytochrome
b5.
Biochemistry 38, 5054-5064.
-
Storch, E.M., Grinstead, J.S., Campbell, A.P., Daggett, V. and
Atkins, W.A. (1999b)
Engineering out motion: A surface disulfide bond alters the mobility of
tryptophan 22 in cytochrome b5 as probed by
time-resolved fluorescence and 1H NMR experiments.
Biochemistry 38, 5065-5075.
-
Sun, Y.-L., Xie, Y., Wang, Y.-H., Xiao, G.-T. and
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The influence of Glu44 and Glu56 of cytochrome b5 on the
protein structure and interaction with cytochrome c.
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Structure, interaction and electron transfer between cytochrome
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Tegoni, M. and Cambillau, C. (1994a)
Structural studies on recombinant and point mutants of flavocytochrome
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Biochimie 76, 501-514.
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Tegoni, M. and Cambillau, C. (1994b)
The 2.6-Å refined structure of the Escherichia coli
recombinant Saccharomyces cerevisiae flavocytochrome
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Tegoni, M., Mozzarelli, A., Rossi, G.L. and Labeyrie, F. (1983)
Complex formation and intermolecular electron transfer between flavocytochrome
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X-ray structure of two complexes of the Y143F flavocytochrome
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Tegoni, M., Gervais, M. and Desbois, A. (1997)
Resonance Raman study on the oxidized and anionic semiquinone forms of
flavocytochrome b2 and L-lactate
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Biochemistry 36, 8932-8946.
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Investigation of the solution structures and mobility of oxidised and
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An analysis of pseudocontact shifts and their relationship to structural
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Methanol-induced unfolding and refolding of cytochrome
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1H and 13C NMR studies of a truncated heme domain from
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Biochim. Biophys. Acta 1382, 129-136
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The identification of cation-binding domains on the surface of
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Importance of a conserved phenylalanine-35 of cytochrome
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Molecular structure of flavocytochrome b2 at 2.4 Å
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Three-dimensional structure of flavocytochrome b2
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Proc. Natl. Acad. Sci. USA 84, 2629-2633.
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Effect of mutation at valine 61 on the three-dimensional structure,
stability, and redox potential of cytochrome b5.
Biochemistry 38, 11961-11972.
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