Source: European journal of biochemistry [Eur J Biochem] 2001 Nov; Vol. 268 (22), pp. 5783-90.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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Academic Journal

Changes to the length of the flexible linker region of the Rieske protein impair the interaction of ubiquinol with the cytochrome bc1 complex.

Authors : Nett JH; Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, USA.; Hunte C

Subjects: Antimycin A/Antimycin A/Antimycin A/*analogs & derivatives ; Electron Transport Complex III/Electron Transport Complex III/Electron Transport Complex III/*chemistry ; Iron-Sulfur Proteins/Iron-Sulfur Proteins/Iron-Sulfur Proteins/*chemistry

Source: European journal of biochemistry [Eur J Biochem] 2000 Sep; Vol. 267 (18), pp. 5777-82.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli.

Authors : Hastings SF; School of Biological and Medical Sciences, University of St Andrews, Scotland, UK.; Kaysser TM

Subjects: Electron Transport Chain Complex Proteins* ; Escherichia coli Proteins*; Cytochromes/Cytochromes/Cytochromes/*metabolism

Source: European journal of biochemistry [Eur J Biochem] 1998 Jul 01; Vol. 255 (1), pp. 317-23.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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Academic Journal

New inhibitors of the ubiquinol oxidase of higher plant mitochondria.

Authors : Hoefnagel MH; Department of Botany, University of Adelaide, Australia.; Wiskich JT

Subjects: Electron Transport Complex III/Electron Transport Complex III/Electron Transport Complex III/*antagonists & inhibitors ; Mitochondria/Mitochondria/Mitochondria/*enzymology ; Plants/Plants/Plants/*enzymology

Source: European journal of biochemistry [Eur J Biochem] 1995 Oct 15; Vol. 233 (2), pp. 531-7.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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Academic Journal

Immunoelectron microscopy and epitope mapping with monoclonal antibodies suggest the existence of an additional N-terminal transmembrane helix in the cytochrome b subunit of bacterial ubiquinol:cytochrome-c oxidoreductases.

Authors : Kleymann G; Max-Planck-Institut für Biophysik, Abteilung Molekulare Membranbiologie, Frankfurt, Germany.; Iwata S

Subjects: Epitope Mapping*; Antibodies, Monoclonal/Antibodies, Monoclonal/Antibodies, Monoclonal/*immunology ; Cytochrome b Group/Cytochrome b Group/Cytochrome b Group/*chemistry

Source: European journal of biochemistry [Eur J Biochem] 1995 May 15; Vol. 230 (1), pp. 359-63.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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Analysis of cytochrome-b amino acid residues forming the contact face with the iron-sulfur subunit of ubiquinol:cytochrome-c reductase in Saccharomyces cerevisiae.

Authors : Giessler A; Universitätsklinikum Frankfurt, Institut für Therapeutische Biochemie, Germany.; Geier BM

Subjects: Amino Acids/Amino Acids/Amino Acids/*analysis ; Cytochrome b Group/Cytochrome b Group/Cytochrome b Group/*chemistry ; Electron Transport Complex III/Electron Transport Complex III/Electron Transport Complex III/*chemistry

Source: European journal of biochemistry [Eur J Biochem] 1994 May 15; Vol. 222 (1), pp. 147-54.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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The C-terminus of the 14-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae is involved in the assembly of a functional enzyme.

Authors : Hemrika W; E.C. Slater Institute, University of Amsterdam, The Netherlands.; De Jong M

Subjects: Genes, Fungal*; Electron Transport Complex III/Electron Transport Complex III/Electron Transport Complex III/*biosynthesis ; Saccharomyces cerevisiae/Saccharomyces cerevisiae/Saccharomyces cerevisiae/*enzymology

Source: European journal of biochemistry [Eur J Biochem] 1994 Mar 01; Vol. 220 (2), pp. 569-76.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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A region of the C-terminal part of the 11-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae contributes to the structure of the Qout reaction domain.

Authors : Hemrika W; E.C. Slater Institute, University of Amsterdam, The Netherlands.; Berden JA

Subjects: Electron Transport Complex III/Electron Transport Complex III/Electron Transport Complex III/*metabolism ; Saccharomyces cerevisiae/Saccharomyces cerevisiae/Saccharomyces cerevisiae/*enzymology; Amino Acid Sequence

Source: European journal of biochemistry [Eur J Biochem] 1993 Aug 01; Vol. 215 (3), pp. 601-9.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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Non-linear inhibition curves for tight-binding inhibitors of dimeric ubiquinol-cytochrome c oxidoreductases. Evidence for rapid inhibitor mobility.

Authors : Bechmann G; Institut für Biochemie, Heinrich-Heine-Universität, Düsseldorf, Federal Republic of Germany.; Weiss H

Subjects: Electron Transport Complex III/Electron Transport Complex III/Electron Transport Complex III/*antagonists & inhibitors; Animals ; Anthraquinones/Anthraquinones/Anthraquinones/pharmacology

Source: European journal of biochemistry [Eur J Biochem] 1992 Sep 01; Vol. 208 (2), pp. 315-25.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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Core I protein of bovine ubiquinol-cytochrome-c reductase; an additional member of the mitochondrial-protein-processing family. Cloning of bovine core I and core II cDNAs and primary structure of the proteins.

Authors : Gencic S; Institut für Therapeutische Biochemie, Universitätsklinikum Frankfurt, Federal Republic of Germany.; Schägger H

Subjects: DNA/DNA/DNA/*genetics ; Electron Transport Complex III/Electron Transport Complex III/Electron Transport Complex III/*genetics ; Nuclear Proteins/Nuclear Proteins/Nuclear Proteins/*genetics

Source: European journal of biochemistry [Eur J Biochem] 1991 Jul 01; Vol. 199 (1), pp. 123-31.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID:

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نتائج البحث

فلترة النتائج

Role of protonatable groups of bovine heart bc(1) complex in ubiquinol binding and oxidation.

Changes to the length of the flexible linker region of the Rieske protein impair the interaction of ubiquinol with the cytochrome bc1 complex.

Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli.

New inhibitors of the ubiquinol oxidase of higher plant mitochondria.

Immunoelectron microscopy and epitope mapping with monoclonal antibodies suggest the existence of an additional N-terminal transmembrane helix in the cytochrome b subunit of bacterial ubiquinol:cytochrome-c oxidoreductases.

Analysis of cytochrome-b amino acid residues forming the contact face with the iron-sulfur subunit of ubiquinol:cytochrome-c reductase in Saccharomyces cerevisiae.

The C-terminus of the 14-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae is involved in the assembly of a functional enzyme.

A region of the C-terminal part of the 11-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae contributes to the structure of the Qout reaction domain.

Non-linear inhibition curves for tight-binding inhibitors of dimeric ubiquinol-cytochrome c oxidoreductases. Evidence for rapid inhibitor mobility.

Core I protein of bovine ubiquinol-cytochrome-c reductase; an additional member of the mitochondrial-protein-processing family. Cloning of bovine core I and core II cDNAs and primary structure of the proteins.

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