B. Ludwig

发表

Lipidomics of intact mitochondria by MALDI-TOF/MS[S]

M. L. Greenberg, A. Corcelli, R. Angelini, 2012, Journal of Lipid Research.

B. Ludwig, 1987 .

Thylakoid-gebundene L-Phenylalanin-Ammoniak-Lyase

W. Löffelhardt, H. Kindl, B. Ludwig, 1973 .

Studying membrane proteins in detergent solution by analytical ultracentrifugation: different methods for density matching

H. Müller, R. Friesen, J. A. V. D. Broek, 1999 .

Sequence homology of bacterial and mitochondrial cytochrome c oxidases. Partial sequence data of cytochrome c oxidase from Paracoccus denitrificans.

W. Oppliger, B. Ludwig, G. Buse, 1983, Biochemical and biophysical research communications.

A novel approach to analyze membrane proteins by laser mass spectrometry: From protein subunits to the integral complex

N. Morgner, B. Ludwig, H. Barth, 2007, Journal of the American Society for Mass Spectrometry.

Letter to the Editor: Complete 1H, 15N and 13C assignment of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state

F. Löhr, H. Rüterjans, C. Lücke, 2000 .

Cytochrome c oxidase--structure, function, and physiology of a redox-driven molecular machine.

B. Ludwig, O-M H Richter, B Ludwig, 2003, Reviews of physiology, biochemistry and pharmacology.

Deciphering protein–protein interactions during the biogenesis of cytochrome c oxidase from Paracoccus denitrificans

P. Gurumoorthy, B. Ludwig, 2015, The FEBS journal.

Two variants of the assembly factor Surf1 target specific terminal oxidases in Paracoccus denitrificans.

K. Hoffmeier, B. Ludwig, F. Bundschuh, 2008, Biochimica et biophysica acta.

Cytochrome c oxidase as a calcium binding protein. Studies on the role of a conserved aspartate in helices XI-XII cytoplasmic loop in cation binding.

C. Soares, B. Ludwig, A. Konstantinov, 2005, Biochemistry.

Reduce to increase: copper binding to a mitochondrial chaperone.

B. Ludwig, 2005, Structure.

Introducing a novel human mtDNA mutation into the Paracoccus denitrificans COX I gene explains functional deficits in a patient

R. Carrozzo, A. Tessa, F. Santorelli, 2006, Neurogenetics.

An oxo‐ferryl tryptophan radical catalytic intermediate in cytochrome c and quinol oxidases trapped by microsecond freeze‐hyperquenching (MHQ)

F. Wiertz, S. de Vries, B. Ludwig, 2004, FEBS letters.

Tyrosine 167: the origin of the radical species observed in the reaction of cytochrome c oxidase with hydrogen peroxide in Paracoccus denitrificans.

H. Michel, A. Kannt, B. Ludwig, 2004, Biochemistry.

A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans.

B. Ludwig, G. Schatz, 1980, Proceedings of the National Academy of Sciences of the United States of America.

Copper and manganese electron spin resonance studies of cytochrome c oxidase from Paracoccus denitrificans.

J. Seelig, A. Seelig, B. Ludwig, 1981, Biochimica et biophysica acta.

Comparison of energy-transducing capabilities of the two- and three-subunit cytochromes aa3 from Paracoccus denitrificans and the 13-subunit beef heart enzyme.

K. Pardhasaradhi, R. Hendler, B. Ludwig, 1991, Biophysical journal.

Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the 13-subunit beef heart enzyme.

K. Pardhasaradhi, R. Hendler, B. Ludwig, 1991, Biophysical journal.

Asp‐193 and Glu‐218 of subunit II are involved in the Mn2+‐binding of Paracoccus denitrificans cytochrome c oxidase

B. Ludwig, E. Bill, B. Kolbesen, 1997, FEBS letters.

Cytochrome-c-binding site on cytochrome oxidase in Paracoccus denitrificans.

M. Brunori, B. Ludwig, F. Malatesta, 1998, European journal of biochemistry.

Electron entry in a CuA mutant of cytochrome c oxidase from Paracoccus denitrificans. Conclusive evidence on the initial electron entry metal center

M. Brunori, V. Zickermann, B. Ludwig, 1998, FEBS letters.

Tryptophan 121 of Subunit II Is the Electron Entry Site to Cytochrome-c Oxidase in Paracoccus denitrificans

M. Brunori, B. Ludwig, F. Malatesta, 1998, The Journal of Biological Chemistry.

Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy.

H. Michel, W. Mäntele, P. Hellwig, 1998, Biochemistry.

Cytochrome c Oxidase (Heme aa3) from Paracoccus denitrificans: Analysis of Mutations in Putative Proton Channels of Subunit I

B. Ludwig, O. Richter, U. Pfitzner, 1998, Journal of bioenergetics and biomembranes.

Single-electron reduction of the oxidized state is coupled to proton uptake via the K pathway in Paracoccus denitrificans cytochrome c oxidase.

E. Bamberg, H. Michel, A. Kannt, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Investigation of the Mn Binding Site in Cytochrome c Oxidase from Paracoccus denitrificans by High-Frequency EPR

B. Ludwig, T. Prisner, F. MacMillan, 2000 .

Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans.

E. Bamberg, H. Michel, A. Kannt, 2000, Biochemistry.

Specificity of the interaction between the Paracoccus denitrificans oxidase and its substrate cytochrome c: comparing the mitochondrial to the homologous bacterial cytochrome c(552), and its truncated and site-directed mutants.

Matthias F. Schneider, B. Ludwig, B. Reincke, 2002, Biochemistry.

Mutations in the docking site for cytochrome c on the Paracoccus heme aa3 oxidase. Electron entry and kinetic phases of the reaction.

B. Ludwig, F. Malatesta, V. Drosou, 2002, European journal of biochemistry.

Vibrational modes of tyrosines in cytochrome c oxidase from Paracoccus denitrificans: FTIR and electrochemical studies on Tyr-D4-labeled and on Tyr280His and Tyr35Phe mutant enzymes.

R. Gennis, H. Michel, W. Mäntele, 2002, Biochemistry.

Cytochrome c oxidase from Paracoccus denitrificans.

B. Ludwig, 1986, Methods in enzymology.

Time-resolved FT-IR studies on the CO adduct of Paracoccus denitrificans cytochrome c oxidase: comparison of the fully reduced and the mixed valence form.

H. Michel, W. Mäntele, P. Hellwig, 1999, Biochemistry.

Role of Surf1 in heme recruitment for bacterial COX biogenesis.

B. Ludwig, F. Bundschuh, A. Hannappel, 2012, Biochimica et biophysica acta.

Structural changes in cytochrome c oxidase induced by cytochrome c binding. A resonance raman study.

J. Hudeček, P. Hildebrandt, B. Ludwig, 2000, Biochimica et biophysica acta.

Comparative resonance Raman study of cytochrome c oxidase from beef heart and Paracoccus denitrificans.

T. Soulimane, P. Hildebrandt, B. Ludwig, 1993, Biochemistry.

Direct Demonstration of Half-of-the-sites Reactivity in the Dimeric Cytochrome bc1 Complex

B. Trumpower, R. Covian, B. Ludwig, 2009, The Journal of Biological Chemistry.

Efficient electron transfer in a protein network lacking specific interactions.

F. Wiertz, H. Heering, Francesca Meschi, 2011, Journal of the American Chemical Society.

Multifrequency pulsed electron paramagnetic resonance on metalloproteins.

U. Brandt, B. Ludwig, T. Maly, 2010, Accounts of chemical research.

Terminal oxidases in Paracoccus denitrificans.

B. Ludwig, 1992, Biochimica et biophysica acta.

Labeling of cytochrome c oxidase with [35S]diazobenzenesulfonate. Orientation of this electron transfer complex in the inner mitochondrial membrane.

N. W. Downer, R. Capaldi, B. Ludwig, 1979, Biochemistry.

A four-subunit cytochrome bc(1) complex complements the respiratory chain of Thermus thermophilus.

M. Karas, T. Soulimane, T. Steiner, 2005, Biochimica et biophysica acta.

True wild type and recombinant wild type cytochrome c oxidase from Paracoccus denitrificans show a 20-fold difference in their catalase activity.

H. Michel, B. Ludwig, I. von der Hocht, 2013, Biochimica et biophysica acta.

Biochemical and Biophysical Characterization of the Two Isoforms of cbb3-Type Cytochrome c Oxidase from Pseudomonas stutzeri

H. Michel, J. Langer, Sabine Buschmann, 2013, Journal of bacteriology.

Expression studies on the ba3 quinol oxidase from Paracoccus denitrificans. A bb3 variant is enzymatically inactive.

B. Ludwig, O. Richter, T. Link, 1997, European journal of biochemistry.

Arrangement of oligomycin-sensitive adenosine triphosphatase in the mitochondrial inner membrane.

R. Capaldi, B. Ludwig, L. Prochaska, 1980, Biochemistry.

Nitric Oxide Reacts with the Single-electron Reduced Active Site of Cytochrome c Oxidase*

M. Brunori, H. Müller, P. Sarti, 2002, The Journal of Biological Chemistry.

Characterization of the CuA center in the cytochrome c oxidase from Thermus thermophilus for the spectral range 1800-500 cm-1 with a combined electrochemical and Fourier transform infrared spectroscopic setup.

M. Wolpert, P. Hellwig, B. Ludwig, 2004, Biopolymers.

Spectroscopic study on the communication between a heme a3 propionate, Asp399 and the binuclear center of cytochrome c oxidase from Paracoccus denitrificans.

W. Mäntele, P. Hellwig, B. Ludwig, 2008, Biochimica et biophysica acta.

Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase

A. Kannt, P. Hellwig, P. Sarti, 2005, The FEBS journal.

Electrochemically induced FT-IR difference spectra of the two- and four-subunit cytochrome c oxidase from P. denitrificans reveal identical conformational changes upon redox transitions.

H. Michel, W. Mäntele, P. Hellwig, 1998, Biochimica et biophysica acta.

Chimeric Quinol Oxidases Expressed in Paracoccus Denitrificans

B. Ludwig, O. Richter, C. Winterstein, 1998 .

A Long-Chain Secondary Alcohol Dehydrogenase from Rhodococcus erythropolis ATCC 4277

B. Ludwig, K. Kendall, A. Akundi, 1995, Applied and environmental microbiology.

Mutational analysis of residues forming hydrogen bonds in the Rieske [2Fe-2S] cluster of the cytochrome bc1 complex in Paracoccus denitrificans.

T. Friedrich, O. Hatzfeld, B. Ludwig, 1998, European journal of biochemistry.

Perturbation of the CuA site in cytochrome-c oxidase of Paracoccus denitrificans by replacement of Met227 with isoleucine.

M. Wikström, M. Verkhovsky, S. Anemüller, 1995, European journal of biochemistry.

Electrochemical and infrared spectroscopic analysis of the interaction of the Cu(A) domain and cytochrome c(552) from Thermus thermophilus.

P. Hellwig, B. Ludwig, J. Fee, 2012, Biochimica et biophysica acta.

Heme aa3-type cytochrome c oxidases from bacteria.

B. Ludwig, Bernd Ludwig, 1980, Biochimica et biophysica acta.

Genes coding for respiratory complexes map on all three chromosomes of the Paracoccus denitrificans genome

B. Ludwig, C. Winterstein, 1998, Archives of Microbiology.

The cytochrome ba3 oxidase from Thermus thermophilus does not generate a tryptophan radical during turnover: Implications for the mechanism of proton pumping.

S. de Vries, B. Ludwig, C. Werner, 2015, Biochimica et biophysica acta.

Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants

H. Michel, A. Kannt, T. Meyer, 2015, FEBS letters.

Cytochromes c550,c552, and c1 in the Electron Transport Network of Paracoccus denitrificans: Redundant or Subtly Different in Function?

H. Westerhoff, R. V. van Spanning, J. van der Oost, 2001, Journal of bacteriology.

A threshold membrane potential accounts for controversial effects of fatty acids on mitochondrial oxidative phosphorylation

B. Ludwig, B. Kadenbach, D. Köhnke, 1993, FEBS letters.

Protein chaperones mediating copper insertion into the CuA site of the aa3-type cytochrome c oxidase of Paracoccus denitrificans.

B. Ludwig, M. Alles, O. Richter, 2015, Biochimica et biophysica acta.

Electron transfer kinetics between soluble modules of Paracoccus denitrificans cytochrome c1 and its physiological redox partners.

B. Ludwig, F. Malatesta, Julia Janzon, 2008, Biochimica et biophysica acta.

Probing the Paracoccus denitrificans cytochrome c 1 / c 552 interaction by mutagenesis and fast kinetics

P. Hellwig, B. Ludwig, F. Malatesta, 2009 .

Probing the Paracoccus denitrificans cytochrome c(1)-cytochrome c(552) interaction by mutagenesis and fast kinetics.

P. Hellwig, B. Ludwig, F. Malatesta, 2008, Biochemistry.

Biochemical and spectroscopic properties of the four-subunit quinol oxidase (cytochrome ba3) from Paracoccus denitrificans.

S. Anemüller, B. Ludwig, O. Richter, 1996, Biochimica et biophysica acta.

Site-directed mutagenesis of cytochrome c oxidase reveals two acidic residues involved in the binding of cytochrome c.

V. Zickermann, B. Ludwig, H. Witt, 1995, Biochimica et biophysica acta.

Paracoccus denitrificans mutants deleted in the gene for subunit II of cytochrome c oxidase also lack subunit I.

B. Ludwig, P. Steinrücke, E. Gerhus, 1991, The Journal of biological chemistry.

Paracoccus denitrificans cytochrome c1 gene replacement mutants

B. Ludwig, P. Steinrücke, E. Gerhus, 1990, Journal of bacteriology.

Surf1, Associated with Leigh Syndrome in Humans, Is a Heme-binding Protein in Bacterial Oxidase Biogenesis*

B. Ludwig, O. Anderka, F. Bundschuh, 2009, The Journal of Biological Chemistry.

Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans

Hartmut Michel, So Iwata, Christian Ostermeier, 1995, Nature.

Rates and Equilibrium of CuA to heme a electron transfer in Paracoccus denitrificans cytochrome c oxidase.

H. Michel, B. Ludwig, O. Farver, 2006, Biophysical journal.

The menaquinol-oxidizing cytochrome bc complex from Thermus thermophilus: protein domains and subunits.

T. Soulimane, B. Ludwig, F. Malatesta, 2006, Biochimica et biophysica acta.

Characterization of heme‐binding properties of Paracoccus denitrificans Surf1 proteins

B. Ludwig, F. Bundschuh, A. Hannappel, 2011, The FEBS journal.

Biogenesis of cytochrome c oxidase--in vitro approaches to study cofactor insertion into a bacterial subunit I.

B. Ludwig, A. Hannappel, C. Werner, 2008, Biochimica et biophysica acta.

The Electron Transfer Complex between Cytochrome c552 and the CuA Domain of the Thermus thermophilus ba3 Oxidase

F. Löhr, H. Rüterjans, Lucia Muresanu, 2006, Journal of Biological Chemistry.

Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex.

F. Wiertz, H. Heering, Francesca Meschi, 2010, Journal of the American Chemical Society.

Different Interaction Modes of Two Cytochrome-c Oxidase Soluble CuA Fragments with Their Substrates*

B. Ludwig, F. Malatesta, O. Maneg, 2003, Journal of Biological Chemistry.

Direct Detection of Fe(IV)=O Intermediates in the Cytochrome aa3 Oxidase from Paracoccus denitrificans/H2O2 Reaction*

Eftychia Pinakoulaki, B. Ludwig, U. Pfitzner, 2003, Journal of Biological Chemistry.

The Protein Effect in the Structure of Two Ferryl-Oxo Intermediates at the Same Oxidation Level in the Heme Copper Binuclear Center of Cytochrome c Oxidase*

Eftychia Pinakoulaki, B. Ludwig, T. Ohta, 2013, The Journal of Biological Chemistry.

Purification and characterization of the cytochrome c oxidase from Rhodopseudomonas sphaeroides.

R. Gennis, A. Azzi, B. Ludwig, 1982, European journal of biochemistry.

Cytochrome c Oxidase Biogenesis and Metallochaperone Interactions: Steps in the Assembly Pathway of a Bacterial Complex

Ilka Wittig, I. Wittig, B. Ludwig, 2017, PloS one.

Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA sequence, gene expression and the protein.

B. Ludwig, G. Buse, G. Steffens, 1987, European journal of biochemistry.

Expression of the Escherichia coli cyo operon in Paracoccus denitrificans results in a fully active quinol oxidase of unexpected heme composition

B. Ludwig, T. Schröter, Christine Winterstein, 1998, FEBS letters.

The cytochromec reductase/oxidase respiratory pathway ofParacoccus denitrificans: Genetic and functional studies

B. Ludwig, P. Steinrücke, E. Gerhus, 1991 .

Genetics ofParacoccus denitrificans

B. Ludwig, Peter SteinrÃ¼cke, 1993 .

Genetics of Paracoccus denitrificans.

B. Ludwig, P. Steinrücke, P. Steinrücke, 1993, FEMS microbiology reviews.

Assembly of Respiratory Complexes I, III, and IV into NADH Oxidase Supercomplex Stabilizes Complex I in Paracoccus denitrificans*

M. Finel, T. Yagi, K. Pfeiffer, 2004, Journal of Biological Chemistry.

Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase.

H. Rüterjans, B. Ludwig, C. Dannehl, 1999, Biochimica et biophysica acta.

Role of copper during carbon monoxide binding to terminal oxidases

B. Ludwig, M. Muntyan, Irmela Zickermann, 1998, FEBS letters.

Asymmetric Binding of Stigmatellin to the Dimeric Paracoccus denitrificans bc1 Complex

B. Trumpower, R. Covian, B. Ludwig, 2007, Journal of Biological Chemistry.

Molecular Genetics of the GenusParacoccus: Metabolically Versatile Bacteria with Bioenergetic Flexibility

R. V. van Spanning, M. D. Page, S. Baker, 1998, Microbiology and Molecular Biology Reviews.

The role of subunit III in bovine cytochrome c oxidase. Comparison between native, subunit III-depleted and Paracoccus denitrificans enzymes.

A. Azzi, B. Ludwig, R. Bolli, 1985, Biochimica et biophysica acta.

Cloning of Paracoccus cytochrome c oxidase subunit II.

B. Ludwig, G. Panskus, B. Paetow, 1985, Journal of inorganic biochemistry.

Dicyclohexylcarbodiimide does not inhibit proton pumping by cytochrome c oxidase of Paracoccus denitrificans.

E. Carafoli, B. Ludwig, M. Solioz, 1983, European journal of biochemistry.

The Role of the Cross-link His-Tyr in the Functional Properties of the Binuclear Center in Cytochrome c Oxidase*

Eftychia Pinakoulaki, B. Ludwig, U. Pfitzner, 2002, The Journal of Biological Chemistry.

Electron transfer kinetics of soluble fragments indicate a direct interaction between complex III and the caa3 oxidase in Thermus thermophilus

B. Ludwig, F. Malatesta, Julia Janzon, 2007, IUBMB life.

Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.

B. Ludwig, M. Jetzek, A. Turba, 1995, European journal of biochemistry.

Synthesis of the Rhodopseudomonas viridis holo-cytochrome c2 in Paracoccus denitrificans.

B. Ludwig, R. Grisshammer, H. Michel, 1993, FEMS microbiology letters.

The genes of the Paracoccus denitrificans bc1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits.

B. Ludwig, B. Kurowski, 1987, The Journal of biological chemistry.

Cytochrome c1 from Paracoccus denitrificans.

B. Ludwig, N. Cerletti, K. Suda, 1983, European journal of biochemistry.

The cytochrome c oxidase of Paracoccus denitrificans pumps protons in a reconstituted system.

E. Carafoli, B. Ludwig, M. Solioz, 1982, The Journal of biological chemistry.

Carboxyl residues in the iron-sulfur protein are involved in the proton pumping activity of P. denitrificans bc(1) complex.

S. Papa, M. Lorusso, T. Cocco, 2001, Biochemistry.

Photoinitiated electron transfer within the Paracoccus denitrificans cytochrome bc1 complex: mobility of the iron-sulfur protein is modulated by the occupant of the Q(o) site.

B. Ludwig, B. Durham, F. Millett, 2011, Biochemistry.

Photo-Initiated Electron Transfer Within the P. denitrificans Cytochrome bc1 Complex: The mobility of the Iron Sulfur Protein is modulated by the occupant of the Qo site†

B. Ludwig, F. Millett, Thomas Kleinschroth, 2011 .

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.

H. Michel, S. Iwata, K. Wiesmüller, 1995, European journal of biochemistry.

Characterization of mutations in crucial residues around the Qo binding site of the cytochrome bc1 complex from Paracoccus denitrificans

P. Hellwig, B. Ludwig, O. Anderka, 2008, The FEBS journal.

X-ray structure of the dimeric cytochrome bc(1) complex from the soil bacterium Paracoccus denitrificans at 2.7-Å resolution.

N. Morgner, C. Hunte, C. Trinh, 2011, Biochimica et biophysica acta.

The structure of porin from Paracoccus denitrificans at 3.1 Å resolution

K. Diederichs, J. Breed, W. Welte, 1997, FEBS letters.

Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase

H. Michel, S. Iwata, C. Ostermeier, 1995, Nature Structural Biology.

Labeling of complex III, with [35S]diazobenzenesulfonate: orientation of this electron transfer segment in the mitochondrial inner membrane.

R. Capaldi, B. Ludwig, R. Bell, 1979, Proceedings of the National Academy of Sciences of the United States of America.

LABELLING OF COMPLEX III WITH 35S DIAZOBENZENESULFONATE. ORIENTATION OF THIS ELECTRON TRANSFER SEGMENT IN THE MITOCHONDRIAL INNER MEMBRANE

R. Capaldi, B. Ludwig, R. Bell, 1978 .

Engineered Fv Fragments as a Tool for the One-Step Purification of Integral Multisubunit Membrane Protein Complexes

H. Michel, C. Ostermeier, B. Ludwig, 1995, Bio/Technology.

A Novel Heme a Insertion Factor Gene Cotranscribes with the Thermus thermophilus Cytochrome ba3 Oxidase Locus

B. Ludwig, O. Richter, C. Werner, 2010, Journal of bacteriology.

Cytochrome c Oxidase and the Regulation of Oxidative Phosphorylation

M. Hüttemann, Icksoo Lee, B. Ludwig, 2001, Chembiochem : a European journal of chemical biology.

Immunoprecipitation of ATP synthetase from beef heart mitochondria.

R. Capaldi, B. Ludwig, 1979, Biochemical and biophysical research communications.

Molecular cloning and functional characterization of the Paracoccus denitrificans porin.

R. Benz, B. Ludwig, K. Saxena, 1997, European journal of biochemistry.

Ion selectivity reversal and induction of voltage-gating by site-directed mutations in the Paracoccus denitrificans porin.

R. Benz, E. Maier, B. Ludwig, 1999, Biochemistry.

Mechanism of Photosynthetic Production and Respiratory Reduction of Molecular Dioxygen: A Biophysical and Biochemical Comparison

G. Renger, B. Ludwig, 2011 .

Transformation of the CuA redox site in cytochrome c oxidase into a mononuclear copper center.

V. Zickermann, B. Ludwig, B Ludwig, 1997, Biochemistry.

The acidic domain of cytochrome c₁ in paracoccus denitrificans, analogous to the acidic subunits in eukaryotic bc₁ complexes, is not involved in the electron transfer reaction to its native substrate cytochrome c(552).

B. Ludwig, F. Malatesta, B. Durham, 2011, Biochimica et biophysica acta.

Electrochemical and ultraviolet/visible/infrared spectroscopic analysis of heme a and a3 redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: separation of heme a and a3 contributions and assignment of vibrational modes.

H. Michel, W. Mäntele, P. Hellwig, 1999, Biochemistry.

Proton slippage in cytochrome c oxidase of Paracoccus denitrificans. Membrane-potential measurements with the two-subunit and three-subunit enzyme.

B. Ludwig, B. Kadenbach, D. Steverding, 1993, European journal of biochemistry.

A Two Subunit Cytochrome c Oxidase from Paracoccus denitrificans

B. Ludwig, 1982 .

Asymmetric binding of the high-affinity Q(H)(*)(-) ubisemiquinone in quinol oxidase (bo3) from Escherichia coli studied by multifrequency electron paramagnetic resonance spectroscopy.

H. Michel, H. Miyoshi, T. Mogi, 2003, Biochemistry.

QH*- ubisemiquinone radical in the bo3-type ubiquinol oxidase studied by pulsed electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy.

H. Michel, B. Ludwig, T. Prisner, 2001, Biochemistry.

FOURIER TRANSFORM INFRARED AND RESONANCE RAMAN STUDIES OF THE INTERACTION OF AZIDE WITH CYTOCHROME C OXIDASE FROM PARACOCCUS DENITRIFICANS

B. Ludwig, Magdalini Vamvouka, C. Varotsis, 1999 .

Mutations in the Ca2+ binding site of the Paracoccus denitrificans cytochrome c oxidase

H. Michel, B. Ludwig, B. Kolbesen, 1999, FEBS letters.

The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin‐arginine translocase

Julie Bachmann, Klaus Zwicker, J. Bachmann, 2006, The FEBS journal.

Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants.

M. Brunori, P. Sarti, B. Ludwig, 2004, Biochemistry.

Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state.

H. Rüterjans, P. Pristovsek, B. Ludwig, 2000, European journal of biochemistry.

Electrochemistry of cytochrome c1, cytochrome c552, and CuA from the respiratory chain of Thermus thermophilus immobilized on gold nanoparticles.

T. Meyer, M. Schmutz, P. Hellwig, 2011, The journal of physical chemistry. B.

Allosteric interactions and proton conducting pathways in proton pumping aa(3) oxidases: heme a as a key coupling element.

S. Papa, N. Capitanio, L. Palese, 2012, Biochimica et biophysica acta.

Kinetic Resolution of a Tryptophan-radical Intermediate in the Reaction Cycle of Paracoccus denitrificans Cytochrome c Oxidase*

F. Wiertz, S. de Vries, B. Ludwig, 2007, Journal of Biological Chemistry.

A D-pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate.

J. Koepke, H. Michel, P. Hellwig, 2008, Journal of molecular biology.

In situ monitoring of the catalytic activity of cytochrome C oxidase in a biomimetic architecture.

W. Knoll, R. Naumann, B. Ludwig, 2008, Biophysical journal.

Thermostability of proteins: role of metal binding and pH on the stability of the dinuclear CuA site of Thermus thermophilus.

S. Mazumdar, A. Sujak, B. Ludwig, 2007, Biophysical journal.

Isolation, Analysis, and Deletion of the Gene Coding for Subunit IV of Cytochrome c Oxidase in Paracoccus denitrificans*

B. Ludwig, H. Witt, 1997, The Journal of Biological Chemistry.

The structure of two ferryl-oxo intermediates at the same oxidation level in the heme-copper binuclear center of cytochrome c oxidase : The protein effect

Eftychia Pinakoulaki, B. Ludwig, T. Ohta, 2013 .

Plant microbody proteins. II. Purification and characterization of the major protein component (SP-63) of peroxisome membranes.

H. Kindl, B. Ludwig, 1976, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

Structure at 1.5 A resolution of cytochrome c(552) with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans.

H. Michel, U. Ermler, B. Ludwig, 2010, Acta crystallographica. Section D, Biological crystallography.

Interaction of cytochrome c with cytochrome oxidase: two different docking scenarios.

B. Ludwig, F. Malatesta, V. Drosou, 2004, Biochimica et biophysica acta.

Asymmetric ATP Hydrolysis Cycle of the Heterodimeric Multidrug ABC Transport Complex TmrAB from Thermus thermophilus*

R. Tampé, U. Hellmich, C. Glaubitz, 2010, The Journal of Biological Chemistry.

Electron transfer and energy transduction in the terminal part of the respiratory chain - lessons from bacterial model systems.

B. Ludwig, O. Richter, 2009, Biochimica et biophysica acta.

Determination of metal-cofactors in enzyme complexes by total-reflection X-ray fluorescence spectrometry

R. Gross, V. Zickermann, B. Ludwig, 1997 .

Mutation of Arg-54 Strongly Influences Heme Composition and Rate and Directionality of Electron Transfer in Paracoccus denitrificans Cytochrome c Oxidase*

H. Michel, W. Mäntele, A. Kannt, 1999, The Journal of Biological Chemistry.

Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.

F. Löhr, H. Rüterjans, H. Wienk, 2003, Biochemistry.

Is a third proton-conducting pathway operative in bacterial cytochrome c oxidase?

B. Ludwig, J. Salje, O. Richter, 2005, Biochemical Society transactions.

Letter to the Editor: Complete 1H, 15N and 13C Assignment of the Soluble Domain of the ba3 Oxidase Subunit II of Thermus Thermophilus in the Reduced State

F. Löhr, H. Rüterjans, B. Ludwig, 2004, Journal of biomolecular NMR.

Subunit II of the Paracoccus denitrificans Cytochrome c Oxidase

B. Ludwig, GUNNAR PANSKUS, PETER STEINRÜCKE, 1988, Annals of the New York Academy of Sciences.

Induction of photochemical auto-reduction of cytochrome-c oxidase by an organic peroxide.

P. Hildebrandt, J. Matysik, B. Ludwig, 2000, Biochimica et biophysica acta.

Cytochrome a3 hemepocket relaxation subsequent to carbon monoxide photolysis from fully reduced cytochrome ba3 oxidase of Paracoccus denitrificans

Eftychia Pinakoulaki, B. Ludwig, T. Ostermann, 1999 .

Protein-protein interactions studied by EPR relaxation measurements: cytochrome c and cytochrome c oxidase.

M. P. D. Vries, B. Ludwig, T. Prisner, 2007, The journal of physical chemistry. B.

The state of association of the cytochrome bc1 complex from Paracoccus denitrificans in solutions of dodecyl maltoside

D. Schubert, B. Ludwig, Gottfried Mayer, 2002 .

Proteo-lipobeads for the oriented encapsulation of membrane proteins.

L. Loew, C. Nowak, P. Frank, 2015, Soft matter.

MALDI-TOF MS lipid profiles of cytochrome c oxidases: cardiolipin is not an essential component of the Paracoccus denitrificans oxidase.

A. Corcelli, R. Angelini, R. Vitale, 2015, Biochemistry.

Structure of the soluble domain of cytochrome c(552) from Paracoccus denitrificans in the oxidized and reduced states.

H. Rüterjans, B. Ludwig, A Harrenga, 2000, Journal of molecular biology.

Terminal oxidases inParacoccus denitrificans

B. Ludwig, 1992 .

Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex.

F. Wiertz, H. Heering, Francesca Meschi, 2010, Journal of the American Chemical Society.

B. Ludwig, F. Malatesta, B. Durham, 2011, Biochimica et biophysica acta.

Solubilized cytochrome c oxidase from Paracoccus denitrificans is a monomer.

A. Lustig, B. Ludwig, J. Rosenbusch, 1982, The Journal of biological chemistry.

Electrochemical and FTIR spectroscopic characterization of the cytochrome bc1 complex from Paracoccus denitrificans: evidence for protonation reactions coupled to quinone binding.

W. Mäntele, P. Hellwig, B. Ludwig, 2003, Biochemistry.