Cyanide-reactive sites in cytochrome bd complex from E. coli (original) (raw)
Infrared and EPR studies on cyanide binding to the heme-copper binuclear center of cytochrome bo-type ubiquinol oxidase from Escherichia coli: Release of a CuB-cyano complex in the partially reduced state
Motonari Tsubaki
Journal of Biological Chemistry
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Heme/heme redox interaction and resolution of individual optical absorption spectra of the hemes in cytochrome bd from Escherichia coli
Tatsushi Mogi
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2009
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EPR studies of the cytochrome-d complex of Escherichia coli
S. Meinhardt
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1989
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Catalytic intermediates of cytochrome bd terminal oxidase at steady-state: Ferryl and oxy-ferrous species dominate
Paolo Sarti
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2011
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Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coli
Tatsushi Mogi
Journal of Biological Chemistry
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Expression of cyoA and cyoB demonstrates that the CO-binding heme component of the Escherichia coli cytochrome o complex is in subunit I
Laura Lemieux
Journal of Biological Chemistry, 1990
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Cyanide-binding Site of bd-type Ubiquinol Oxidase from Escherichia coli
Tatsushi Mogi
Journal of Biological Chemistry, 1995
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Low temperature EPR and MCD studies on cytochrome b-558 of the Bacillus subtilis succinate: quinone oxidoreductase indicate bis-histidine coordination of the heme iron
K Kristoffer Andersson
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
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Axial heme ligation in the cytochrome bc1 complexes of mitochondrial and photosynthetic membranes. A near-infrared magnetic circular dichroism and electron paramagnetic resonance study
Michael Finnegan
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1996
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Ligand binding to the haem-copper binuclear catalytic site of cytochrome bo, a respiratory quinol oxidase from Escherichia coli
Janet Horrocks
European Journal of Biochemistry, 1993
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Reaction of E. coli catalase HPII with cyanide as ligand and as inhibitor
C. Obinger
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
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Redox control of fast ligand dissociation from Escherichia coli cytochrome bd
Paolo Sarti
Biochemical and Biophysical Research Communications, 2007
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Oxygenated complex of cytochrome bd from Escherichia coli: Stability and photolability
Ilya Belevich
FEBS Letters, 2005
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A re-examination of the reactions of cyanide with cytochrome c oxidase
David Bickar
Biochemical Journal, 1984
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Cyanide binding and active site structure in heme-copper oxidases: Normal coordinate analysis of iron-cyanide vibrations of CN− complexes of cytochromesba3 andaa3
Kristene Surerus
Biospectroscopy, 1998
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Extended Heme Promiscuity in the Cyanobacterial Cytochrome c Oxidase: Characterization of Native Complexes Containing Hemes A, O, and D, Respectively
Marnik Wastyn
Archives of Biochemistry and Biophysics, 1999
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Probing the oxygen binding site of cytochrome c oxidase with cyanide
Paolo Sarti, Giovanni Antonini
Journal of Inorganic Biochemistry, 1993
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Cytochrome d axial ligand of the bd-type terminal quinol oxidase from Escherichia coli
Tatsushi Mogi, Motonari Tsubaki
FEBS Letters, 1993
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The binding of cyanide to cytochrome d in intact cells, spheroplasts, membrane fragments and solubilized enzyme from Salmonella typhimurium
Dariush Minai-Tehrani
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2001
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Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: EPR and Fourier transform infrared spectroscopic studies
Tatsushi Mogi
Biochemistry, 1993
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Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site
Alexander Konstantinov
Proceedings of the National Academy of Sciences, 2005
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Assignment of ESR signals of Escherichia coli terminal oxidase complexes
清司 古西
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1985
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Circular dichroism spectra of cytochrome c oxidase
A. Dyuba, Alexander Konstantinov
Metallomics, 2011
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A re-examination of the reactions of cyanide with cytochrome c oxidase
David Bickar
Biochemical Journal, 1984
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Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli
John Hill
Proceedings of the National Academy of Sciences, 1993
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Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: Amino acid substitutions for two histidines that are putative CuB ligands
Laura Lemieux
Biochemistry, 1993
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Inhibition by cyanide of the respiratory chain oxidases of Escherichia coli
Philip Bragg
Archives of Biochemistry and Biophysics, 1974
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Spontaneous spectral changes of the reduced cytochrome bd
Alexander Konstantinov
FEBS Letters, 1997
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Low‐Temperature EPR and Mössbauer Spectroscopy of Two Cytochromes with His–Met Axial Coordination Exhibiting HALS Signals
Stefano Ciurli
…, 2006
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Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli
Laura Lemieux, James O Alben
Biochemistry, 1993
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The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies
Erik Sedlák
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2004
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Redox Properties of Wild-Type and Heme-Binding Loop Mutants of Bacterial Cytochromes c Measured by Direct Electrochemistry
Ravinder Kaur
Inorganic Chemistry, 2005
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Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa 3 and cytochrome bo
christos georgiou
Journal of Bioenergetics and Biomembranes, 1993
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