Bruce Mackler

University of Wisconsin–Madison, Madison, Wisconsin, United States

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Publications (10)53.23 Total impact

  • Nathar Penn · Bruce Mackler
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    ABSTRACT: A particulate DPNH cytochrome c reductase has been isolated from beef liver microsomes in highly purified form. Preparations of the enzyme contained per mg protein an average of 2.1 · 10−3μM flavin, 5.3 · 10−3μM cytochrome b5, and 2.6 · 10−3μM non-heme iron. Lipide accounted for 71% of the total dry weight. The enzyme catalyzed the oxidation of 50 μmoles of DPNH per min/mg enzyme protein by ferricyanide and 30 μmoles per min/mg by cytochrome c. Enzymic activity was inhibited by p-chloromercuribenzoate, but was unaffected by antimycin, A amytal and chelating agents.
    Biochimica et Biophysica Acta 04/1958; 27(3):539-43. DOI:10.1016/0006-3002(58)90383-4 · 4.66 Impact Factor
  • Bruce Mackler · Nathar Penn
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    ABSTRACT: DPNH oxidase has been fragmented with mixtures of chocolate, ammonium sulfate and trypsin into a red particle with DPNH cytochrome c reductase activity (antimycin sensitive) and a green particle with cytochrome oxidase activity. This fragmentation probably accounts for the opening phenomenon in which the DPNH-oxidase activity of DPNH oxidase is abolished by exposure to deoxycholate, and two new activities emerge, viz. DPNH-cytochrome c reductase activity and ferrocytochrome c oxidase activity.
    Biochimica et Biophysica Acta 06/1957; 24(24):294-300. DOI:10.1016/0006-3002(57)90197-X · 4.66 Impact Factor
  • D E GREEN · Bruce Mackler
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    ABSTRACT: The preparation of two modified forms of the electron transport particle (ETP) has been described. One form (closed) can catalyze only to a slight degree the oxidation of DPNH by ferricytochrome c or the oxidation of ferrocytochrome c by oxygen except after exposure to desoxycholate. As these two activities emerge the capacity to catalyze the over-all DPNH-oxygen reaction is lost. This latter activity is restored by the addition of small amounts of cytochrome c. The second form approximates the behavior of the closed form which had been exposed to desoxycholate.
    Biochimica et Biophysica Acta 08/1956; 21(1):1-6. DOI:10.1016/0006-3002(56)90086-5 · 4.66 Impact Factor
  • D E GREEN · B MACKLER
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    ABSTRACT: Some enzymic properties and the composition of two modified forms (I and II) of the electron transport particle (ETP) have been examined. Such preparations contain per mg of protein 0.42·10−3 μmole of flavin, 2.5·10−3 μmoles of heme, 6.2·10−3 μmoles of non-heme iron and 2.4·10−3 μmoles of copper—the molecular or atomic ratios being in round numbers 1:6:15:6. The antimycin titer of the preparations was 0.5·10−3 μmole/mg. The oxido-reduction of the prosthetic hemes in presence of DPNH and oxygen has been demonstrated. Heme reduction was partially inhibited by antimycin. The absorption spectrum of the enzyme indicates the presence of at least two groups of hemes—one group with bands at 563, 554, 535 and 525 mμ—the other with a band at 603 mμ.
    Biochimica et Biophysica Acta 08/1956; 21(1):6-13. · 4.66 Impact Factor
  • Bruce Mackler · D.E. Green
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    ABSTRACT: Some enzymic properties and the composition of two modified forms (I and II) of the electron transport particle (ETP) have been examined. Such preparations contain per mg of protein 0.42·10−3 μmole of flavin, 2.5·10−3 μmoles of heme, 6.2·10−3 μmoles of non-heme iron and 2.4·10−3 μmoles of copper—the molecular or atomic ratios being in round numbers 1:6:15:6. The antimycin titer of the preparations was 0.5·10−3 μmole/mg. The oxido-reduction of the prosthetic hemes in presence of DPNH and oxygen has been demonstrated. Heme reduction was partially inhibited by antimycin. The absorption spectrum of the enzyme indicates the presence of at least two groups of hemes—one group with bands at 563, 554, 535 and 525 mμ—the other with a band at 603 mμ.
    Biochimica et Biophysica Acta 07/1956; 21(1):6-13. DOI:10.1016/0006-3002(56)90087-7 · 4.66 Impact Factor
  • H. R. Mahler · Alan S. Fairhurst · Bruce Mackler
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    ABSTRACT: In an attempt to elucidate the function of the metal in metalloflavoproteins two experimental approaches have been used : a study of the interaction of seven different pure flavoproteins, both metal-containing and metal-free, with a series of quinones of widely varying oxido-reduction potentials ; and an investigation of some of the properties and reactions of riboflavinmetal chelates, as models of metalloflavoproteins. The first approach has led to the recognition of two characteristic constants for flavoproteins, the optimal interaction potential (ε) and the reaction constant (κ). A comparison of metal-free and metal-containing enzymes reveals that the presence of metal leads to a shift in ε and a decrease in κ. The study of the model system has disclosed that the oxidation of DPNH by cytochrome-c in the presence of diaphorase is specifically stimulated by ferririboflavin, The rate of this reaction is further enhanced if the ferririboflavin is chelated with aromatic, but not with aliphatic, iron-binding agents. Some of the theoretical and practical implication of these findings especially as they relate to electron transport and oxidative phosphorylation are discussed.
    Journal of the American Chemical Society 03/1955; 77(6). DOI:10.1021/ja01611a035 · 11.44 Impact Factor
  • Bruce Mackler · R REPASKE · P M KOHOUT · D E GREEN
    Biochimica et Biophysica Acta 12/1954; 15(3):437-8. DOI:10.1016/0006-3002(54)90050-5 · 4.66 Impact Factor
  • D E GREEN · Bruce Mackler · R REPASKE · H R MAHLER
    Biochimica et Biophysica Acta 11/1954; 15(3):435-7. DOI:10.1016/0006-3002(54)90049-9 · 4.66 Impact Factor
  • Source
    H R MAHLER · B MACKLER · D E GREEN
    Journal of Biological Chemistry 10/1954; 210(1):465-80. · 4.57 Impact Factor
  • Bruce Mackler · H. R. Mahler · D. E. Green
    Journal of Biological Chemistry 09/1954; 210(1). · 4.57 Impact Factor