scholarly journals Mechanisms of Nitric Oxide Reactions Mediated by Biologically Relevant Metal Centers

2013 ◽  
pp. 99-135 ◽  
Author(s):  
Peter C. Ford ◽  
Jose Clayston Melo Pereira ◽  
Katrina M. Miranda
Keyword(s):  
Nitric Oxide ◽  
Metal Centers ◽  
Biologically Relevant

REACTION MECHANISMS OF NITRIC OXIDE WITH BIOLOGICALLY RELEVANT METAL CENTERS

2003 ◽  
pp. 203-257 ◽  
Author(s):  
PETER C. FORD ◽  
LEROY E. LAVERMAN ◽  
IVAN M. LORKOVIC
Keyword(s):  
Nitric Oxide ◽  
Reaction Mechanisms ◽  
Metal Centers ◽  
Biologically Relevant

scholarly journals Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species

Antioxidants ◽  
2019 ◽  
Vol 8 (2) ◽  
pp. 48 ◽  
Author(s):  
Dayana Benchoam ◽  
Ernesto Cuevasanta ◽  
Matías Möller ◽  
Beatriz Alvarez
Keyword(s):  
Hydrogen Sulfide ◽  
Oxidation Products ◽  
Physiological Effects ◽  
Metal Centers ◽  
Biologically Relevant ◽  
Mammalian Tissues ◽  
Sulfenic Acids ◽  
Electrophilic Character

Hydrogen sulfide (H2S/HS–) can be formed in mammalian tissues and exert physiological effects. It can react with metal centers and oxidized thiol products such as disulfides (RSSR) and sulfenic acids (RSOH). Reactions with oxidized thiol products form persulfides (RSSH/RSS–). Persulfides have been proposed to transduce the signaling effects of H2S through the modification of critical cysteines. They are more nucleophilic and acidic than thiols and, contrary to thiols, also possess electrophilic character. In this review, we summarize the biochemistry of hydrogen sulfide and persulfides, focusing on redox aspects. We describe biologically relevant one- and two-electron oxidants and their reactions with H2S and persulfides, as well as the fates of the oxidation products. The biological implications are discussed.

Tyrosine confounds oxidative electrochemical detection of nitric oxide

1998 ◽  
Vol 274 (5) ◽  
pp. H1698-H1704 ◽  
Author(s):  
R. Stingele ◽  
D. A. Wilson ◽  
R. J. Traystman ◽  
D. F. Hanley
Keyword(s):  
Nitric Oxide ◽  
Blood Brain Barrier ◽  
Electrochemical Detection ◽  
Concentration Gradient ◽  
Brain Barrier ◽  
Future Studies ◽  
Biologically Relevant ◽  
Blood Brain ◽  
Dog Brain ◽  
Order Of Magnitude

We report evidence that a porphyrinic microsensor for detection of nitric oxide (NO) also detects biologically relevant concentrations of tyrosine (Tyr) in dog brain. Tyr is oxidized by this sensor at the same potential as NO, and the sensitivity for NO and Tyr are of the same order of magnitude. The interference from Tyr is of importance because 1) Tyr is abundant and 2) there is a concentration gradient of Tyr across the blood-brain barrier that can lead to unpredictable results if disturbed by ischemia or hypoxia. The knowledge of this interference is important for the interpretation of results obtained with this sensor and for the design of future studies.

Reactivity pathways for nitric oxide and nitrosonium with iron complexes in biologically relevant sulfur coordination spheres

2007 ◽  
Vol 101 (11-12) ◽  
pp. 1730-1738 ◽  
Author(s):  
Todd C. Harrop ◽  
Datong Song ◽  
Stephen J. Lippard
Keyword(s):  
Nitric Oxide ◽  
Iron Complexes ◽  
Biologically Relevant ◽  
Coordination Spheres

scholarly journals Nitric oxide rapidly scavenges tyrosine and tryptophan radicals

1995 ◽  
Vol 310 (3) ◽  
pp. 745-749 ◽  
Author(s):  
J P Eiserich ◽  
J Butler ◽  
A van der Vliet ◽  
C E Cross ◽  
B Halliwell
Keyword(s):  
Nitric Oxide ◽  
Biologically Relevant ◽  
Tyrosine Residues ◽  
Transfer Processes ◽  
Diffusion Controlled ◽  
Electron Transfer Processes ◽  
Protein Radicals ◽  
First Time

By utilizing a pulse-radiolytic technique, we demonstrate for the first time that the rate constant for the reaction of nitric oxide (.NO) with biologically relevant tyrosine and tryptophan radicals (Tyr. and Trp. respectively) in amino acids, peptides and proteins is of the order of (1-2) x 10(9) M-1.s-1. We also show that .NO effectively interferes with electron-transfer processes between tryptophan and tyrosine residues in proteins subjected to pulse radiolysis. The near diffusion-controlled rates of these reactions, coupled with the increasingly recognized role of protein radicals in enzyme catalysis and oxidative damage, suggest that Tyr. and Trp. are likely and important targets for .NO generated in vivo.

scholarly journals A system for exposing molecules and cells to biologically relevant and accurately controlled steady-state concentrations of nitric oxide and oxygen

Nitric Oxide ◽  
2012 ◽  
Vol 27 (3) ◽  
pp. 161-168 ◽  
Author(s):  
Vasileios Dendroulakis ◽  
Brandon S. Russell ◽  
C. Eric Elmquist ◽  
Laura J. Trudel ◽  
Gerald N. Wogan ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Steady State ◽  
Biologically Relevant

The contribution of metalloporphyrin complexes in molecular sensing and in sustainable polymerization processes: a new and unique perspective.

2021 ◽  
Author(s):  
Maria Strianese ◽  
Daniela Pappalardo ◽  
Mina MAZZEO ◽  
Marina Lamberti ◽  
Claudio Pellecchia
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Sulfide ◽  
Optical Probes ◽  
Molecular Sensing ◽  
Biologically Relevant ◽  
Recent Developments ◽  
Biologically Relevant Molecules

This review highlights the recent developments in the field of metalloporphyrins as optical probes for biologically relevant molecules, such as nitric oxide (NO) and hydrogen sulfide (H2S), and as catalysts...

scholarly journals The porphyrin ring rather than the metal ion dictates long-range electron transport across proteins suggesting coherence-assisted mechanism

2020 ◽  
Vol 117 (51) ◽  
pp. 32260-32266
Author(s):  
Yuval Agam ◽  
Ramesh Nandi ◽  
Alexander Kaushansky ◽  
Uri Peskin ◽  
Nadav Amdursky
Keyword(s):  
Long Range ◽  
Metal Ion ◽  
Electron Mediator ◽  
Metal Centers ◽  
Biologically Relevant ◽  
Natural Systems ◽  
Redox Center ◽  
Fundamental Biological Process ◽  
Metal Redox ◽  
Electron Mediators

The fundamental biological process of electron transfer (ET) takes place across proteins with common ET pathways of several nanometers. Recent discoveries push this limit and show long-range extracellular ET over several micrometers. Here, we aim in deciphering how protein-bound intramolecular cofactors can facilitate such long-range ET. In contrast to natural systems, our protein-based platform enables us to modulate important factors associated with ET in a facile manner, such as the type of the cofactor and its quantity within the protein. We choose here the biologically relevant protoporphyrin molecule as the electron mediator. Unlike natural systems having only Fe-containing protoporphyrins, i.e., heme, as electron mediators, we use here porphyrins with different metal centers, or lacking a metal center. We show that the metal redox center has no role in ET and that ET is mediated solely by the conjugated backbone of the molecule. We further discuss several ET mechanisms, accounting to our observations with possible contribution of coherent processes. Our findings contribute to our understanding of the participation of heme molecules in long-range biological ET.

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