J
Jonathan B. Wittenberg
Researcher at Albert Einstein College of Medicine
Publications - 80
Citations - 5480
Jonathan B. Wittenberg is an academic researcher from Albert Einstein College of Medicine. The author has contributed to research in topics: Heme & Hemoglobin. The author has an hindex of 44, co-authored 80 publications receiving 5351 citations. Previous affiliations of Jonathan B. Wittenberg include Marine Biological Laboratory & Yeshiva University.
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Structural characterization of a group II 2/2 hemoglobin from the plant pathogen Agrobacterium tumefaciens
Alessandra Pesce,Marco Nardini,Marie LaBarre,Christian Richard,Jonathan B. Wittenberg,Beatrice A. Wittenberg,Michel Guertin,Martino Bolognesi +7 more
TL;DR: The first structural characterization of a group II 2/2Hb from the soil and phytopathogenic bacterium Agrobacterium tumefaciens (At-2/2 HbO) is presented, adding new distinctive information to the complex picture of currently available 2/ 2Hb structural and functional data.
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Leghemoglobin: the role of hemoglobin in the nitrogen-fixing legume root nodule*
TL;DR: The molecular mechanism by which leghemoglobin augments the oxygen consumption and nitrogen-fixing activity of bacteroids is inquired into, and facilitated diffusion makes oxygen more available to the terminal oxidases of subcellular organelles.
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Leghemoglobin I. CHANGES IN CONFORMATION AND CHEMICAL REACTIVITY LINKED TO REACTION WITH ACETIC ACID
TL;DR: In this article, it was shown that in the presence of acetic acid, the rate of reduction of leghemoglobin α by dithionite is proportional to the fraction of uncombined leghemogen.
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Hemoglobin Kinetics of the Galapagos Rift Vent Tube Worm Riftia pachyptila Jones (Pogonophora; Vestimentifera).
TL;DR: Kinetics of the reactions of Riftia pachyptila hemoglobin with oxygen were followed spectrophotometrically by stopped-flow and laser flash photolysis techniques, finding that the oxygen affinity is relatively temperature independent.
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Circular dichroism spectroscopy of Lucina I hemoglobin
TL;DR: The monomeric hemoglobin from the mollusc Lucina pectinata (HbI) represents an interesting model system for the study of heme‐related circular dichroic (CD) bands in view of the highly asymmetric distribution of aromatic residues around the heme pocket revealed by the X‐ray crystal structure.