M
Michael J. Barber
Researcher at University of South Florida
Publications - 114
Citations - 3895
Michael J. Barber is an academic researcher from University of South Florida. The author has contributed to research in topics: Nitrate reductase & Flavin group. The author has an hindex of 34, co-authored 113 publications receiving 3819 citations. Previous affiliations of Michael J. Barber include University of Bristol & Virginia Tech.
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Journal ArticleDOI
Assimilatory nitrate reductase: functional properties and regulation
TL;DR: This chapter discusses Functional Size and Quaternary Structure, Functional Domains, Immunological Properties, Molecular Biology and Derived Primary Structures, and Active Site Residues.
Journal ArticleDOI
The Pro-Apoptotic Proteins, Bid and Bax, Cause a Limited Permeabilization of the Mitochondrial Outer Membrane That Is Enhanced by Cytosol
Ruth M. Kluck,Mauro Dogli Esposti,Guy Perkins,Christian Renken,Tomomi Kuwana,Ella Bossy-Wetzel,Martin W. Goldberg,Terence D Allen,Michael J. Barber,Douglas R. Green,Donald D. Newmeyer +10 more
TL;DR: It is hypothesized that PEF activity could help determine whether cells can recover from mitochondrial cytochrome c release, as outer membrane permeability was strikingly increased by a macromolecular cytosolic factor, termed PEF (permeability enhancing factor).
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Bid-induced cytochrome c release is mediated by a pathway independent of mitochondrial permeability transition pore and Bax.
TL;DR: Bid possesses the biochemical activity to induce cytochrome c release through a mechanism independent of mitochondrial permeability transition pore and Bax, and the two proteins could function synergistically.
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Changes in apparent pH on freezing aqueous buffer solutions and their relevance to biochemical electron-paramagnetic-resonance spectroscopy.
TL;DR: It is concluded that apparent pH changes of up to about 3pH units may occur under particular conditions, and it is recommended that as a prelude to future detailed low-temperature biochemical work, appropriate tests with an indicator system should be performed.
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Oxidation-reduction potentials of molybdenum, flavin and iron-sulphur centres in milk xanthine oxidase.
TL;DR: The mid-point reduction potentials of the various groups in xanthine oxidase from bovine milk were determined by potentiometric titration with dithionite in the presence of dye mediators, removing samples for quantification of the reduced species byelectron-paramagnetic-resonance spectroscopy.