A singular value decomposition approach for kinetic analysis of reactions of HNO with myoglobin

Zapata, Adrian; Kumar, Murugaeson R.; Pervitsky, Dmitry; Farmer, Patrick J.

doi:10.1016/j.jinorgbio.2012.10.005

Cited by 16 publications

(17 citation statements)

References 43 publications

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“…In terms of reactivity, competitive trapping experiments were performed by reaction of Mb−NHO with excess CO gas to monitor the replacement of HNO. Here, the rate constants for HNO binding and dissociation were reported as 4.2 × 10 9 M –1 s –1 and 8.9 × 10 –5 s –1 , respectively . The unimolecular loss of HNO from Mb was determined to be independent of CO concentration.…”

Section: The Nitrogen Cyclementioning

confidence: 94%

“…The unimolecular loss of HNO from Mb was determined to be independent of CO concentration. On the other hand, the bimolecular rate constant for CO binding to Mb was reported to be 5.1 × 10 5 M –1 s –1 . The small rate constant for HNO release from Mb compared to the fast binding constant of CO indicates that HNO dissociation is the rate limiting step.…”

Section: The Nitrogen Cyclementioning

confidence: 99%

“…The slow dissociation of HNO is proposed to originate from hydrogen-bond stabilization of the ligand in the distal pocket of Mb, as discussed above (see Figure ). , …”

Section: The Nitrogen Cyclementioning

confidence: 99%

“…In contrast, reaction of HNO with ferric heme proteins, for example met-Mb/Hb, leads to HNO deprotonation upon coordination to the ferric heme, followed by electron transfer, ultimately generating stable ls-{FeNO} 7 complexes. , …”

Section: The Nitrogen Cyclementioning

confidence: 99%

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The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

et al. 2021

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Nitric oxide (NO) is an important signaling molecule that is involved in a wide range of physiological and pathological events in biology. Metal coordination chemistry, especially with iron, is at the heart of many biological transformations involving NO. A series of heme proteins, nitric oxide synthases (NOS), soluble guanylate cyclase (sGC), and nitrophorins, are responsible for the biosynthesis, sensing, and transport of NO. Alternatively, NO can be generated from nitrite by heme- and copper-containing nitrite reductases (NIRs). The NO-bearing small molecules such as nitrosothiols and dinitrosyl iron complexes (DNICs) can serve as an alternative vehicle for NO storage and transport. Once NO is formed, the rich reaction chemistry of NO leads to a wide variety of biological activities including reduction of NO by heme or non-heme iron-containing NO reductases and protein post-translational modifications by DNICs. Much of our understanding of the reactivity of metal sites in biology with NO and the mechanisms of these transformations has come from the elucidation of the geometric and electronic structures and chemical reactivity of synthetic model systems, in synergy with biochemical and biophysical studies on the relevant proteins themselves. This review focuses on recent advancements from studies on proteins and model complexes that not only have improved our understanding of the biological roles of NO but also have provided foundations for biomedical research and for bio-inspired catalyst design in energy science.

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Section: The Nitrogen Cyclementioning

confidence: 94%

Section: The Nitrogen Cyclementioning

confidence: 99%

“…The slow dissociation of HNO is proposed to originate from hydrogen-bond stabilization of the ligand in the distal pocket of Mb, as discussed above (see Figure ). , …”

Section: The Nitrogen Cyclementioning

confidence: 99%

Section: The Nitrogen Cyclementioning

confidence: 99%

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The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

et al. 2021

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“…It can also be oxidized to • NO [ E ] ° ( • NO / HNO ) = − 0.14 V [ 1 ], recently revised as E° ( • NO / HNO ) = 0.27 V [ 2 ]. HNO reacts with molecular oxygen, [ 3 – 9 ], nitric oxide [ 10 ], nitrite [ 11 , 12 ], hydroxylamine [ 12 , 13 ], sulfite [ 12 ], thiosulfate [ 12 , 13 ], metalloproteins [ 14 – 18 ], metalloporphyrines [ 19 – 22 ], thiols [ 3 , 13 , 14 , 23 ], C- and S-nitroso compounds [ 12 , 24 ], nitroxides [ 13 , 25 – 27 ] and phosphines [ 12 , 13 , 28 – 33 ]. Thiols constitute the main biological target of HNO [ 34 ].…”

Section: Introductionmentioning

confidence: 99%

Kinetics of Azanone (HNO) Reactions with Thiols: Effect of pH

Smulik-Izydorczyk

Dębowska

Adamus

et al. 2021

Cell Biochem Biophys

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HNO (nitroxyl, IUPAC name azanone) is an electrophilic reactive nitrogen species of growing pharmacological and biological significance. Here, we present data on the pH-dependent kinetics of azanone reactions with the low molecular thiols glutathione and N-acetylcysteine, as well as with important serum proteins: bovine serum albumin and human serum albumin. The competition kinetics method used is based on two parallel HNO reactions: with RSH/RS− or with O2. The results provide evidence that the reaction of azanone with the anionic form of thiols (RS−) is favored over reactions with the protonated form (RSH). The data are supported with quantum mechanical calculations. A comprehensive discussion of the HNO reaction with thiolates is provided.

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Synthesis, characterization and CO-releasing property of palladium(II) bipyridine flavonolate complexes

2019

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A singular value decomposition approach for kinetic analysis of reactions of HNO with myoglobin

Cited by 16 publications

References 43 publications

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

Kinetics of Azanone (HNO) Reactions with Thiols: Effect of pH

Synthesis, characterization and CO-releasing property of palladium(II) bipyridine flavonolate complexes

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