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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Myoglobin function reassessed.
TL;DR: The heart and those striated muscles that contract for long periods, having available almost limitless oxygen, operate in sustained steady states of low sarcoplasmic oxygen pressure that resist change in response to changing muscle work or oxygen supply.
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Truncated Hemoglobins: A New Family of Hemoglobins Widely Distributed in Bacteria, Unicellular Eukaryotes, and Plants
TL;DR: Crystal structures show that trHb tertiary structure is based on a 2-on-2 -hel-ical sandwich, which represents an unprecedented editing of the highly conserved globin fold, and may provide a path for ligand diffusion to the heme.
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Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide.
Hugues Ouellet,Yannick Ouellet,Christian Richard,Marie LaBarre,Beatrice A. Wittenberg,Jonathan B. Wittenberg,Michel Guertin +6 more
TL;DR: It is reported that disruption of M. bovis bacillus Calmette–Guérin glbN caused a dramatic reduction in the NO-consuming activity of stationary phase cells, and that activity could be restored fully by complementing knockout cells withglbN, and an NO-metabolizing activity in M. tuberculosis or M.bovis is demonstrated.
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A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis
Manon Couture,Syun Ru Yeh,Beatrice A. Wittenberg,Jonathan B. Wittenberg,Yannick Ouellet,Denis L. Rousseau,Michel Guertin +6 more
TL;DR: The results suggest that, physiologically, the primary role of HbN may be to protect the bacilli against reactive nitrogen species produced by the host macrophage.
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Facilitated oxygen diffusion. The role of leghemoglobin in nitrogen fixation by bacteroids isolated from soybean root nodules.
TL;DR: It is deduced that oxyleghemoglobin and other oxygenbinding proteins exert their effects by facilitating the diffusion of oxygen through a thin layer of solution, the "unstirred layer," surrounding the bacteroids, which results in the "effective" oxygen uptake which supports nitrogenase activity.