Search Results - "Mauk, A G"

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  1. 1

    The Peroxidase Activity of a Hemin−DNA Oligonucleotide Complex:  Free Radical Damage to Specific Guanine Bases of the DNA by Travascio, Paola, Witting, Paul K, Mauk, A. Grant, Sen, Dipankar

    Published in Journal of the American Chemical Society (21-02-2001)
    “…A specific DNA oligonucleotide−hemin complex (PS2.M−hemin complex) that exhibits DNA-enhanced peroxidative activity was studied by EPR and UV−visible…”
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  2. 2

    Acid-Induced Denaturation of Myoglobin Studied by Time-Resolved Electrospray Ionization Mass Spectrometry by Konermann, L, Rosell, F. I, Mauk, A. G, Douglas, D. J

    Published in Biochemistry (Easton) (27-05-1997)
    “…The acid-induced denaturation of holo-myoglobin (hMb) following a pH-jump from 6.5 to 3.2 has been studied by electrospray ionization (ESI) mass spectrometry…”
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  3. 3

    Tandem mass spectrometry of protein-protein complexes: Cytochrome c-cytochrome b5 by MAUK, M. R, MAUK, A. G, CHEN, Yu-Luan, DOUGLAS, D. J

    “…An improved method to interpret triple quadrupole MS/MS experiments of complexes of large ions is presented and applied to a study of the complex formed by the…”
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  4. 4

    A DNA Oligonucleotide−Hemin Complex Cleaves t-Butyl Hydroperoxide through a Homolytic Mechanism by Witting, Paul K, Travascio, Paula, Sen, Dipankar, Mauk, A. Grant

    Published in Inorganic chemistry (10-09-2001)
    “…Both electron paramagnetic resonance (EPR) and electronic absorption spectroscopy have been employed to investigate the reaction of a guanine-rich DNA…”
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  5. 5

    Cytochrome c Peroxidase−Cytochrome c Complex:  Locating the Second Binding Domain on Cytochrome c Peroxidase with Site-Directed Mutagenesis by Leesch, Valerie W, Bujons, Jordi, Mauk, A. Grant, Hoffman, Brian M

    Published in Biochemistry (Easton) (22-08-2000)
    “…Cytochrome c peroxidase (CcP) can bind as many as two cytochrome c (Cc) molecules in an electrostatic complex. The location of the two binding domains on CcP…”
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  6. 6

    Characterization of an Alkaline Transition Intermediate Stabilized in the Phe82Trp Variant of Yeast iso-1-Cytochrome c by Rosell, Federico I, Harris, Thomas R, Hildebrand, Dean P, Döpner, Susanne, Hildebrandt, Peter, Mauk, A. Grant

    Published in Biochemistry (Easton) (01-08-2000)
    “…In general, mutation of the phylogenetically conserved residue Phe82 in yeast iso-1-cytochrome c destabilizes the native conformation of the protein by…”
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  7. 7

    Characterization of BphF, a Rieske-Type Ferredoxin with a Low Reduction Potential by Couture, Manon M.-J, Colbert, Christopher L, Babini, Elena, Rosell, Federico I, Mauk, A. Grant, Bolin, Jeffrey T, Eltis, Lindsay D

    Published in Biochemistry (Easton) (09-01-2001)
    “…BphF is a small, soluble, Rieske-type ferredoxin involved in the microbial degradation of biphenyl. The rapid, anaerobic purification of a heterologously…”
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  8. 8

    Monooxygenase activity of cytochrome c peroxidase by MILLER, V.P, DEPILLIS, G. D, FERRER, J. C, MAUK, A. G, ORTIZ DE MONTELLANO, P. R

    Published in The Journal of biological chemistry (05-05-1992)
    “…Recombinant cytochrome c peroxidase (CcP) and a W51A mutant of CcP, in contrast to other classical peroxidases, react with phenylhydrazine to give sigma-bonded…”
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  9. 9

    Directed evolution of copper nitrite reductase to a chromogenic reductant by MacPherson, Iain S., Rosell, Federico I., Scofield, Melanie, Mauk, A. Grant, Murphy, Michael E.P.

    Published in Protein engineering, design and selection (01-03-2010)
    “…Directed evolution methods were developed for Cu-containing nitrite reductase (NiR) from Alcaligenes faecalis S-6. The PCR cloning strategy allows for the…”
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  10. 10

    Responses of two protein-protein complexes to solvent stress: does water play a role at the interface? by Kornblatt, J.A., Kornblatt, M.J., Hoa, G.H., Mauk, A.G.

    Published in Biophysical journal (01-09-1993)
    “…We have analyzed the stability of the cytochrome c-cytochrome b5 and cytochrome c-cytochrome c oxidase complexes as a function of solvent stress. High…”
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  11. 11

    Small substrates and cytochrome c are oxidized at different sites of cytochrome c peroxidase by DEPILLIS, G. D, SISHTA, B. P, MAUK, A. G, ORTIZ DE MONTELLANO, P. R

    Published in The Journal of biological chemistry (15-10-1991)
    “…Modeling studies suggest that electrons are transferred from cytochrome c to cytochrome c peroxidase (CcP) with cytochrome c predominantly bound at a site…”
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  12. 12

    Laser flash photolysis studies of electron transfer to the cytochrome b5-cytochrome c complex by Meyer, T. E, Rivera, M, Walker, F. A, Mauk, M. R, Mauk, A. G, Cusanovich, M. A, Tollin, G

    Published in Biochemistry (Easton) (19-01-1993)
    “…Rate constants for electron transfer in the complex between recombinant rat mitochondrial outer membrane cytochrome b5 or the tryptic fragment of bovine liver…”
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  13. 13

    Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis by Davies, Anne M, Guillemette, J. Guy, Smith, Michael, Greenwood, Colin, Thurgood, Andrew G. P, Mauk, A. Grant, Moore, Geoffrey R

    Published in Biochemistry (Easton) (25-05-1993)
    “…Heme propionate-7 in cytochrome c is an ionizable group located in a region of the protein that is inaccessible to bulk solvent. Electrostatic stabilization of…”
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  14. 14

    Transmutation of a Heme Protein by Barker, Paul D., Ferrer, Juan C., Mylrajan, Muthusamy, Loehr, Thomas M., Feng, Rong, Konishi, Yasuo, Funk, Walter D., Ross T. A. Mac Gillivray, Mauk, A. Grant

    “…Residue Asn57of bovine liver cytochrome b5has been replaced with a cysteine residue, and the resulting variant has been isolated from recombinant Escherichia…”
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  15. 15

    The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51 by Goodin, D B, Mauk, A G, Smith, M

    Published in The Journal of biological chemistry (05-06-1987)
    “…The nature of the free radical species observed in the peroxide complex of yeast cytochrome c peroxidase is described for protein variants containing amino…”
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  16. 16

    Resonance Raman study of the interactions between cytochrome c variants and cytochrome c oxidase by Hildebrandt, Peter, Vanhecke, Franck, Buse, Gerhard, Soulimane, Tewfik, Mauk, A. Grant

    Published in Biochemistry (Easton) (12-10-1993)
    “…The structural changes in oxidized yeast iso-1-cytochrome c and fully oxidized bovine cytochrome c oxidase that are induced upon complex formation have been…”
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  17. 17

    Bacterial Expression of a Mitochondrial Cytochrome c. Trimethylation of Lys72 in Yeast iso-1-Cytochrome c and the Alkaline Conformational Transition by Pollock, W. Brent R, Rosell, Federico I, Twitchett, Mark B, Dumont, Mark E, Mauk, A. Grant

    Published in Biochemistry (Easton) (28-04-1998)
    “…Saccharomyces cerevisiae iso-1-cytochrome c has been expressed in Escherichia coli by coexpression of the genes encoding the cytochrome (CYC1) and yeast…”
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  18. 18

    Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants by Liang, N, Pielak, G.J, Mauk, A.G, Smith, M, Hoffman, B.M

    “…Of the many factors known to influence the rate of electron transfer between two metalloproteins, it is particularly difficult to assess the role of the…”
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  19. 19

    Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: effects on coordination, species preference for cytochrome c, and electron transfer by Goodin, David B, Davidson, Marilyn G, Roe, James A, Mauk, A. Grant, Smith, Michael

    Published in Biochemistry (Easton) (01-05-1991)
    “…Amino acid replacements of an aromatic residue, Trp-51, which is in contact with the heme of yeast cytochrome c peroxidase have a number of significant effects…”
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  20. 20

    Models for the complexes formed between cytochrome b5 and the subunits of methemoglobin by Poulos, T L, Mauk, A G

    Published in The Journal of biological chemistry (25-06-1983)
    “…Computer graphics-generated models for the electron transfer complexes formed between cytochrome b5 and the subunits of methemoglobin are proposed. For both…”
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