An unusual hemoprotein capable of reversible binding of nitric oxide from the gram-positive Bacillus halodenitrificans

1994 ◽  
Vol 162 (5) ◽  
pp. 316-322 ◽  
Author(s):  
Gerard Denariaz ◽  
Paul A. Ketchum ◽  
William J. Payne ◽  
Ming-Yih Liu ◽  
Jean LeGall ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Gram Positive ◽  
Reversible Binding

An unusual hemoprotein capable of reversible binding of nitric oxide from the gram-positive Bacillus halodenitrificans

1994 ◽  
Vol 162 (5) ◽  
pp. 316-322 ◽  
Author(s):  
Gerard Denariaz ◽  
P. A. Ketchum ◽  
William J. Payne ◽  
Ming-Yih Liu ◽  
J. LeGall ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Gram Positive ◽  
Reversible Binding

Reversible binding of nitric oxide and carbon monoxide to iron porphyrins. Assessment of the role of the protein in hemoglobin

1973 ◽  
Vol 95 (12) ◽  
pp. 4087-4089 ◽  
Author(s):  
Dennis V. Stynes ◽  
H. Cleary. Stynes ◽  
Brian R. James ◽  
James A. Ibers
Keyword(s):  
Nitric Oxide ◽  
Carbon Monoxide ◽  
Iron Porphyrins ◽  
Reversible Binding

scholarly journals Mechanism of Gram-positive Shock: Identification of Peptidoglycan and Lipoteichoic Acid Moieties Essential in the Induction of Nitric Oxide Synthase, Shock, and Multiple Organ Failure

1998 ◽  
Vol 188 (2) ◽  
pp. 305-315 ◽  
Author(s):  
Ken M. Kengatharan ◽  
Sjef De Kimpe ◽  
Caroline Robson ◽  
Simon J. Foster ◽  
Christoph Thiemermann
Keyword(s):  
Nitric Oxide ◽  
Multiple Organ Failure ◽  
Organ Failure ◽  
Lipoteichoic Acid ◽  
Interferon Γ ◽  
Multiple Organ ◽  
Organ Injury ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
No Formation

The incidence of septic shock caused by gram-positive bacteria has risen markedly in the last few years. It is largely unclear how gram-positive bacteria (which do not contain endotoxin) cause shock and multiple organ failure. We have discovered recently that two cell wall fragments of the pathogenic gram-positive bacterium Staphylococcus aureus, lipoteichoic acid (LTA) and peptidoglycan (PepG), synergize to cause the induction of nitric oxide (NO) formation, shock, and organ injury in the rat. We report here that a specific fragment of PepG, N-acetylglucosamine-β-[1→ 4]-N-acetylmuramyl-l-alanine–d-isoglutamine, is the moiety within the PepG polymer responsible for the synergism with LTA (or the cytokine interferon γ) to induce NO formation in the murine macrophage cell line J774.2. However, this moiety is also present in the PepG of the nonpathogenic bacterium Bacillus subtilis. We have discovered subsequently that S. aureus LTA synergizes with PepG from either bacterium to cause enhanced NO formation, shock, and organ injury in the rat, whereas the LTA from B. subtilis does not synergize with PepG of either bacterium. Thus, we propose that the structure of LTA determines the ability of a particular bacterium to cause shock and multiple organ failure (pathogenicity), while PepG acts to amplify any response induced by LTA.

Mechanistic Studies on the Reversible Binding of Nitric Oxide to Metmyoglobin

2001 ◽  
Vol 123 (2) ◽  
pp. 285-293 ◽  
Author(s):  
Leroy E. Laverman ◽  
Alicja Wanat ◽  
Janusz Oszajca ◽  
Grazyna Stochel ◽  
Peter C. Ford ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Mechanistic Studies ◽  
Reversible Binding

scholarly journals Susceptibility of Gram-positive and -negative bacteria to novel nitric oxide-releasing nanoparticle technology

Virulence ◽  
2011 ◽  
Vol 2 (3) ◽  
pp. 217-221 ◽  
Author(s):  
Adam Friedman ◽  
Karin Blecher ◽  
David Sanchez ◽  
Chaim Tuckman-Vernon ◽  
Philip Gialanella ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Gram Positive ◽  
Nitric Oxide Releasing
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