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The High-Molecular-Weight Cytochrome c Cyc2 of Acidithiobacillus ferrooxidans Is an Outer Membrane Protein

Journal of Bacteriology, 2002-01, Vol.184 (1), p.313-317

2002

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QO Site Deficiency Can Be Compensated by Extragenic Mutations in the Hinge Region of the Iron-Sulfur Protein in the bc1 Complex of Saccharomyces cerevisiae

The Journal of biological chemistry, 2004-06, Vol.279 (23), p.24203-24211

2004

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A proposed Common Training Framework for Specialists in Laboratory Medicine under EU Directive 2013/55/EC (The Recognition of Professional Qualifications)

Clinical chemistry and laboratory medicine, 2021-02, Vol.59 (3), p.505-512

2021

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Is Cytochrome b Glutamic Acid 272 a Quinol Binding Residue in the bc 1 Complex of Saccharomyces cerevisiae?

Biochemistry (Easton), 2008-02, Vol.47 (8), p.2357-2368

2008

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Identification of membrane-bound c-type cytochromes in an acidophilic ferrous ion oxidizing bacterium Thiobacillus ferrooxidans

FEMS microbiology letters, 1996-02, Vol.136 (1), p.51-56

1996

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Paclitaxel induces release of cytochrome c from mitochondria isolated from human neuroblastoma cells

Cancer research (Chicago, Ill.), 2000-10, Vol.60 (19), p.5349-5353

2000

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The bc1 complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction : Is there a second bc1 complex?

Biochimica et biophysica acta. Bioenergetics, 2002-09, Vol.1555 (1), p.37-43

2002

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Is Cytochrome b Glutamic Acid 272 a Quinol Binding Residue in the bc1 Complex of Saccharomyces cerevisiae?

Biochemistry (Easton), 2008-02, Vol.47 (8), p.2357-2368

2008

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Is Cytochrome b Glutamic Acid 272 a Quinol Binding Residue in the bc sub(1) Complex of Saccharomyces cerevisiae?

Biochemistry (Easton), 2008-01, Vol.47 (8), p.2357-2368

2008

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Inhibitor Binding within the NarI Subunit (Cytochromebnr) of Escherichia coli Nitrate Reductase A

The Journal of biological chemistry, 1998-05, Vol.273 (18), p.10851-10856

1998

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Early Evolution of Cytochrome bc Complexes

Journal of Molecular Biology, 2000-07, Vol.300 (4), p.663-675

2000

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The bc(1) complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction. Is there a second bc(1) complex?

Biochimica et biophysica acta, 2002-09, Vol.1555 (1-3), p.37

2002

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S15.13 Is cytochrome b glutamic acid 272 a quinol binding residue in the bc1 complex?

Biochimica et biophysica acta. Bioenergetics, 2008-07, Vol.1777, p.S105-S105

2008

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Redox Components of Cytochrome bc-type Enzymes in Acidophilic Prokaryotes

The Journal of biological chemistry, 1999-06, Vol.274 (24), p.16766-16772

1999

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Redox Components of Cytochrome bc-type Enzymes in Acidophilic Prokaryotes

The Journal of biological chemistry, 1999-06, Vol.274 (24), p.16760-16765

1999

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Role of the Evolutionarily Conserved Cytochrome b Tryptophan 142 in the Ubiquinol Oxidation Catalyzed by the bc1 Complex in the Yeast Saccharomyces cerevisiae(∗)

The Journal of biological chemistry, 1995-09, Vol.270 (38), p.22321-22328

1995

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Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms

The Journal of biological chemistry, 1999-06, Vol.274 (24), p.16766-16772

1999

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Heme Axial Ligation by the Highly Conserved His Residues in Helix II of Cytochrome b (NarI) of Escherichia coliNitrate Reductase A (NarGHI)

The Journal of biological chemistry, 1997-10, Vol.272 (41), p.25652-25658

1997

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Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. I. Characterization of the cytochrome bc1-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans

The Journal of biological chemistry, 1999-06, Vol.274 (24), p.16760-16765

1999

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The bc1 complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction

Biochimica et biophysica acta. Bioenergetics, 2002-09, Vol.1555 (1-3), p.37-43

2002

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Analysis of suppressor mutation reveals long distance interactions in the bc1 complex of Saccharomyces cerevisiae

Biochimica et biophysica acta. Bioenergetics, 2001-08, Vol.1506 (2), p.89-102

2001

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Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A

The Journal of biological chemistry, 1997-10, Vol.272 (41), p.25652-25658

1997

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Identification of membrane-bound c-type cytochromes in an acidophilic ferrous ion oxidizing bacterium Thiobacillus ferrooxidans

FEMS microbiology letters, 1996-02, Vol.136 (1), p.51-56

1996

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The High-Molecular-Weight Cytochrome c Cyc2 of Acidithiobacillus ferrooxidans Is an Outer Membrane Protein

Journal of bacteriology, 2002-03, Vol.184 (5), p.1502-1502

2002

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Decoupling of the bc1 complex in S. cerevisiae; point mutations affecting the cytochrome b gene bring new information about the structural aspect of the proton translocation

Journal of bioenergetics and biomembranes, 1995-10, Vol.27 (5), p.527

1995

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The High-Molecular-Weight Cytochrome c Cyc2 of Acidithiobacillus ferrooxidans Is an Outer Membrane Protein

QO Site Deficiency Can Be Compensated by Extragenic Mutations in the Hinge Region of the Iron-Sulfur Protein in the bc1 Complex of Saccharomyces cerevisiae

A proposed Common Training Framework for Specialists in Laboratory Medicine under EU Directive 2013/55/EC (The Recognition of Professional Qualifications)

Is Cytochrome b Glutamic Acid 272 a Quinol Binding Residue in the bc 1 Complex of Saccharomyces cerevisiae?

Identification of membrane-bound c-type cytochromes in an acidophilic ferrous ion oxidizing bacterium Thiobacillus ferrooxidans

Paclitaxel induces release of cytochrome c from mitochondria isolated from human neuroblastoma cells

The bc1 complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction : Is there a second bc1 complex?

Is Cytochrome b Glutamic Acid 272 a Quinol Binding Residue in the bc1 Complex of Saccharomyces cerevisiae?

Is Cytochrome b Glutamic Acid 272 a Quinol Binding Residue in the bc sub(1) Complex of Saccharomyces cerevisiae?

Inhibitor Binding within the NarI Subunit (Cytochromebnr) of Escherichia coli Nitrate Reductase A

Early Evolution of Cytochrome bc Complexes

The bc(1) complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction. Is there a second bc(1) complex?

S15.13 Is cytochrome b glutamic acid 272 a quinol binding residue in the bc1 complex?

Redox Components of Cytochrome bc-type Enzymes in Acidophilic Prokaryotes

Redox Components of Cytochrome bc-type Enzymes in Acidophilic Prokaryotes

Role of the Evolutionarily Conserved Cytochrome b Tryptophan 142 in the Ubiquinol Oxidation Catalyzed by the bc1 Complex in the Yeast Saccharomyces cerevisiae(∗)

Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms

Heme Axial Ligation by the Highly Conserved His Residues in Helix II of Cytochrome b (NarI) of Escherichia coliNitrate Reductase A (NarGHI)

Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. I. Characterization of the cytochrome bc1-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans

The bc1 complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction

Analysis of suppressor mutation reveals long distance interactions in the bc1 complex of Saccharomyces cerevisiae

Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A

Identification of membrane-bound c-type cytochromes in an acidophilic ferrous ion oxidizing bacterium Thiobacillus ferrooxidans

The High-Molecular-Weight Cytochrome c Cyc2 of Acidithiobacillus ferrooxidans Is an Outer Membrane Protein

Decoupling of the bc1 complex in S. cerevisiae; point mutations affecting the cytochrome b gene bring new information about the structural aspect of the proton translocation

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