Nitric Oxide Research from Chemistry to Biology

Henry, Y.; Guissani, Annie; Ducastel, Béatrice

doi:10.1007/978-1-4613-1185-0

Cited by 34 publications

(7 citation statements)

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“…Ferrous heme–nitrosyl complexes generally have S t = 1/2 ground states, which is evident from their EPR spectra . Early work studying ferrous heme–nitrosyls in both model complexes and proteins like Hb and Mb laid the ground work for characterizing these species, as summarized in Table . ,,,,,, EPR spectra of 5C ls-{FeNO} 7 complexes generally display g values of ∼2.10, 2.06, and 2.01, as shown in Figure , which compares the EPR spectra of the Fe(II)–NO adduct of sGC and the model complex [Fe(T o -F 2 PP)(NO)] . [Fe(OEP)(NO)] was investigated using single crystal EPR spectroscopy and it was found that the principal axis of the minimum g value, g min , is closely aligned with the Fe–NO bond and therefore corresponds to g z …”

Section: Nitric Oxide In Mammalian Signaling and Immune Defensementioning

confidence: 91%

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: Nitric Oxide In Mammalian Signaling and Immune Defensementioning

confidence: 91%

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

et al. 2021

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“…acid (Beligni et al, 2002). This reaction may occur under microlocalized pH conditions in the chloroplast and apoplastic space, where ascorbic acid is known to be present (Henry et al, 1997).…”

Section: Common Sites Of Ros and No Production Within Plant Cellsmentioning

confidence: 99%

Cross‐talk of Reactive Oxygen Species and Nitric Oxide in Various Processes of Plant Development

Kolbert

Feigl

2017

Reactive Oxygen Species in Plants

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What does the 'x' stand for here? AQ2 Do you mean Kim et al. 2006 as listed in the References section? AQ3 Pls define 'PTM' here. AQ4 Explain/define this? AQ5 Only 2009 listed for these authors; check? AQ6 Pls check my 'key' to abbreviations and insert definition for 'PA'. AQ7 Spelling: should be 'phytoglobin'? AQ8 Check my expansion of ABA here. AQ9 In what sense 'intensification'? do you mean 'upregulation'? AQ10 Do you mean Desel & Krupinska 2005 as listed? AQ11 Sense? Do you mean 'suggesting' or 'evidencing' maybe? AQ12 Sense not clear; pls check. AQ13 Do you mean Tsukagoshi et al. 2010 as listed? AQ14 Pls define/gloss 'PIN' here. AQ15 Sense: do you mean 'inactivating NADPH oxidase'? AQ16 Check text as edited. AQ17 Sense not clear; pls rephrase. AQ18 Do you mean 'ripened'? AQ19 Pls can you supply a page range for the section/chapter cited? AQ20 Pls supply names and initials of editors for this book if possible.

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“…P450s) to oxidatively convert l -arginine to citrulline and NO. − The NO produced in this way in neurons and the endothelium is then sensed by the enzyme soluble guanylate cyclase (sGC), which uses a heme as the primary NO-sensor unit. − Similar sensor domains, termed H-NOX, are also found in bacteria as gas sensors (primarily for O 2 and NO). − In bacteria, NO is produced by bacterial NOS, and the NO generated in this way is then involved in quorum sensing and potentially biosynthesis . In humans, NO is further degraded in blood by reaction with oxy-hemoglobin (by oxidation to nitrate), to avoid accumulation of this toxic molecule. − Other important heme proteins involved in the biological functions of NO are nitrophorins (NO transporters in the saliva of blood-sucking insects), , and heme-based nitrite and NO reductases (NIRs and NORs), responsible for the production and detoxification of NO in denitrification. − Heme-NO adducts are further important intermediates in a number of key reactions in the nitrogen cycle. − Correspondingly, much research has been directed toward the interaction of NO with hemes, in proteins and model systems, and the study of the geometric and electronic structures as well as the reactivity of these species in different oxidation states. ,− Initially, studies focused on ferrous heme-nitrosyls, or {FeNO} 7 complexes in the Enemark–Feltham notation, as models for the corresponding O 2 adducts of heme proteins. − Later, these {FeNO} 7 complexes turned out to be the relevant species involved in NO-based signaling. , In the Enemark–Feltham notation, the exponent “7” corresponds to the number of valence electrons of the complex, which is the sum of Fe(d) and NO(π*) electrons (here: 6 for Fe(II) plus 1 for NO = 7). This notation is useful, because NO is a “noninnocent” or redox-active ligand, , and hence, it is a priori not clear what the electron distribution in a given transition metal-NO complex is.…”

Section: Introductionmentioning

confidence: 99%

Activation of Non-Heme Iron-Nitrosyl Complexes: Turning Up the Heat

et al. 2019

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The chemistry of nonheme iron centers with NO in different oxidation states has experienced a renaissance in the last 10 years because of recent findings of their involvement in N2O generation (in nitric oxide reductases – NORs), dinitrosyl iron complex (DNIC) formation, NO sensing in transcription factors, and the biosynthesis of natural products that contain N-nitroso groups. Using model complexes, great strides have been made in our understanding of the reactivity and electronic structures of nonheme iron-nitrosyl complexes in different oxidation states, and yet there is much more to be learned. Whereas many nonheme, high-spin (hs) {FeNO}7 complexes, formed from the reaction of NO with Fe(II), have been prepared and thoroughly characterized (although even in this case, their ability to directly couple two NO to N2O in dinuclear systems had been overlooked for a long time), much less is known about nonheme iron-nitrosyl complexes in other oxidation states, especially hs-{FeNO}6 and hs-{FeNO}8. In both of these cases, very few examples have been reported, and the reactivity of these complexes is largely unexplored. This is an exciting area of coordination chemistry that warrants more attention in the field.

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Nitric Oxide Research from Chemistry to Biology

Cited by 34 publications

References 0 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

Cross‐talk of Reactive Oxygen Species and Nitric Oxide in Various Processes of Plant Development

Activation of Non-Heme Iron-Nitrosyl Complexes: Turning Up the Heat

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