Thiyl free radicals and the oxidation of ferrocytochrome <i>c</i> Direct observation of coupled hydrogen-atom- and electron-transfer reactions

Forni, Luigi G.; Willson, R. L.

doi:10.1042/bj2400905

Cited by 37 publications

(11 citation statements)

References 18 publications

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“…In our last reported work, we observed a similar trend which was accounted for the production of azidyl radical [18]. This azidyl radical is considered more reactive and reported to oxidize many compounds including thiol and phenol [40][41][42][43]. Benzoquinone is considered to lower the reaction rate by scavenging superoxide [44][45][46].…”

Section: Mechanistic Study For the Presence Of Main Reactive Oxygen Ssupporting

confidence: 69%

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Controlled leaching with prolonged activity for Co–LDH supported catalyst during treatment of organic dyes using bicarbonate activation of hydrogen peroxide

Ali

Lü

et al. 2015

Journal of Hazardous Materials

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Section: Mechanistic Study For the Presence Of Main Reactive Oxygen Ssupporting

confidence: 69%

“…Actually, NaN 3 is reported to react with both singlet oxygen and • OH through Eqs. (3) and (4) as their rate constants are nearly close to each other (2 × 10 9 vs 1 × 10 10 M −1 s −1 ) [40][41][42][43].…”

Section: Mechanistic Study For the Presence Of Main Reactive Oxygen Smentioning

confidence: 78%

Controlled leaching with prolonged activity for Co–LDH supported catalyst during treatment of organic dyes using bicarbonate activation of hydrogen peroxide

Ali

Lü

et al. 2015

Journal of Hazardous Materials

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“…It is the reducing agent used by the GPX/GR system for the regeneration of GSH from its oxidized form GSSG [59]. It may act as a direct antioxidant by reducing glutathiyl and tyrosyl radicals generated during oxidative stress [60;61]. It can directly absorb UVR [46;62].…”

Section: Resultsmentioning

confidence: 99%

Corneal aldehyde dehydrogenases: Multiple functions and novel nuclear localization

Stagos

Chen

Cantore

et al. 2010

Brain Research Bulletin

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Aldehyde dehydrogenases (ALDHs) represent a superfamily of NAD(P)+-dependent enzymes which catalyze the oxidation of a wide variety of endogenous and exogenous aldehydes to their corresponding acids. Some ALDHs have been identified as corneal crystallins and thereby contribute to the protective and refractive properties of the cornea. ALDH3A1 is highly expressed in the cornea of most mammals with the exception of rabbit, who abundantly expresses ALDH1A1 in the cornea instead of ALDH3A1. In this study, we examined the gene expression of other ALDHs and found high messenger levels of ALDH1B1, ALDH2 and ALDH7A1 in mouse cornea and lens. Substantial evidence supports a protective role for ALDH3A1 and ALDH1A1 against ultraviolet radiation (UVR)-induced oxidative damage to ocular tissues. The mechanism by which this protection occurs includes UVR filtering, detoxification of reactive aldehydes generated by UVR exposure and antioxidant activity. We recently have identified ALDH3A1 as a nuclear protein in corneal epithelium. Herein, we show that ALDH3A1 is also found in the nucleus of rabbit keratocytes. The nuclear presence of ALDH3A1 may be involved in cell cycle regulation.

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“…The occurrence of reaction (2) would indicate that RSS' species may be even weaker one-electron oxidants than Fe(mii)-cytochrome-c (E°(Fe(iii)cytc/Fe(ii)cytc)=0 . 27 V), in contrast to RS' species which readily oxidize Fe(ii)cytc (Forni and Willson 1986) . Just before proof-reading of this paper a study was published (Everett et al .…”

Section: Introductionmentioning

confidence: 85%

Catalytic Reduction of Fe(III)-cytochrome-cInvolving Stable Radiolysis Products Derived from Disulphides, Proteins and Thiols

1992

International Journal of Radiation Biology

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gamma-Radiolysis, with doses less than 1 kGy, of aqueous solutions of disulphides, disulphide-proteins or thiols leads to the generation of stable products, capable of stimulating the catalytic reduction of Fe(III)-cytochrome-c by unirradiated glutathione, and by other thiols. The stimulatory activity fades within 20-60 min in the case of irradiated thiols, but there was little loss of this activity when irradiated solutions of disulphides or disulphide-proteins were stored at 4 degrees C for days. Disulphides (e.g. cystamine) are mainly activated by .OH radicals, disulphide-proteins (e.g. alpha-chymotrypsin) mainly by e-aq, and thiols (e.g. cysteine) by virtually all water radicals. The radiolytic activation, which is only partially prevented by oxygen, can be attributed to the generation of trace amounts of higher sulphides and persulphides (RSSSR, RSSSSR and RSSH). Such species are known to stimulate Fe(III)-cytochrome-c reduction by glutathione in a chain reaction (Massey et al. 1971). The radiolytic stimulation of reductive catalytic activity of thiols and disulphides may play a role in irradiated biological systems, and might be exploited to identify irradiated proteins with Fe(III)-cytochrome-c as detector.

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Thiyl free radicals and the oxidation of ferrocytochrome c Direct observation of coupled hydrogen-atom- and electron-transfer reactions

Cited by 37 publications

References 18 publications

Controlled leaching with prolonged activity for Co–LDH supported catalyst during treatment of organic dyes using bicarbonate activation of hydrogen peroxide

Controlled leaching with prolonged activity for Co–LDH supported catalyst during treatment of organic dyes using bicarbonate activation of hydrogen peroxide

Corneal aldehyde dehydrogenases: Multiple functions and novel nuclear localization

Catalytic Reduction of Fe(III)-cytochrome-cInvolving Stable Radiolysis Products Derived from Disulphides, Proteins and Thiols

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