Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Nagao, Shigeaki; Asami, Osamu; Yasui, Hiroyuki; Hirota, Shun

doi:10.1016/j.bbapap.2011.01.008

Cited by 9 publications

(10 citation statements)

References 33 publications

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“…To evaluate the effect of ribose glycation on HMb's function, we performed kinetic studies by reaction of the protein with H 2 O 2 . As shown in Figure 6A, upon mixing with H 2 O 2 , the met ribosylated HMb rapidly converted from met (Fe III ) to ferryl form (Fe IV =O, 420 and 588 nm), similar to those observed in previous studies [22,29]. By fitting the decay of the Sort band to the single-exponential function, the obtained k obs values for the formation of ferryl heme were linearly dependent on the concentration of H 2 O 2 (Figure 6B).…”

Section: Stopped-flow Kinetic Studiessupporting

confidence: 86%

“…Molecules 2021, 26, x FOR PEER REVIEW 7 of 11 from met (Fe III ) to ferryl form (Fe IV =O, 420 and 588 nm), similar to those observed in previous studies [22,29]. By fitting the decay of the Sort band to the single-exponential function, the obtained kobs values for the formation of ferryl heme were linearly dependent on the concentration of H2O2 (Figure 6B).…”

Section: Stopped-flow Kinetic Studiessupporting

confidence: 85%

“…The HMb was expressed in E. Coli. BL21(DE3) cells and purified using a protocol as previously reported [ 29 ]. To test the protein glycation of the HMb, we performed reactions with the d -ribose or d -glucose at 37 °C, pH 7.0, for 1–24 h. The UV-Vis spectra of the reaction solution were recorded at 1, 4, 8, 12, and 24 h, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…Shun Hirota, Nara Institute of Science and Technology (NAIST), Japan. The protein was expressed in BL21(DE3) and purified using a procedure described in the literature [ 29 ]. The purity of the HMb was confirmed by the mass spectrum and the ratio between the absorbance at 280 and 409 nm (Abs 409nm /Abs 280nm > 5.0).…”

Section: Methodsmentioning

confidence: 99%

“…Comparatively, the protein glycation of other globins in the organism, such as myoglobin ((Mb), Figure 1 , left), is less studied [ 20 , 21 , 22 , 23 , 24 ]. In addition to the biological function of O 2 storage and transportation, Mb may also exhibit multiple biological functions, such as serving as a nitric oxide (NO) scavenger and a hypoxic nitrite reductase (NIR) [ 25 , 26 , 27 ], as well as a peroxidase using H 2 O 2 as an oxidant [ 28 , 29 ]. Mb mainly exists in the cytoplasm of cardiomyocytes and in skeletal muscle cells.…”

Section: Introductionmentioning

confidence: 99%

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Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose

et al. 2021

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Protein glycation is an important protein post-translational modification and is one of the main pathogenesis of diabetic angiopathy. Other than glycated hemoglobin, the protein glycation of other globins such as myoglobin (Mb) is less studied. The protein glycation of human Mb with ribose has not been reported, and the glycation sites in the Mb remain unknown. This article reports that d-ribose undergoes rapid protein glycation of human myoglobin (HMb) at lysine residues (K34, K87, K56, and K147) on the protein surface, as identified by ultra-high performance liquid chromatography-mass spectrometry (UHPLC-MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). Moreover, glycation by d-ribose at these sites slightly decreased the rate of the met heme (FeIII) in reaction with H2O2 to form a ferryl heme (FeIV=O). This study provides valuable insight into the protein glycation by d-ribose and provides a foundation for studying the structure and function of glycated heme proteins.

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Section: Stopped-flow Kinetic Studiessupporting

confidence: 86%

Section: Stopped-flow Kinetic Studiessupporting

confidence: 85%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose

et al. 2021

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Reactivity toward oxygen radicals and antioxidant action of thiol compounds

Takashima¹,

Shichiri²,

Hagihara³

et al. 2012

BioFactors

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Thiol compounds exert diverse functions in the defense network against oxidative stress in vivo. Above all, the role of glutathione in the enzymatic removal of hydrogen peroxide and lipid hydroperoxides has been well established. The scavenging of reactive free radicals is one of the many functions. In this study, the reactivities of several thiol compounds toward oxygen- and nitrogen-centered radicals were measured from their reaction with galvinoxyl and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radicals and also from their sparing effects on the decay of fluorescein, pyrogallol red, and BODIPY induced by peroxyl radicals. Furthermore, the antioxidant capacity against lipid peroxidation was assessed in the oxidation of methyl linoleate induced by free radicals in micelle systems. Cysteine, homocysteine, and glutathione exhibited considerable reactivity toward galvinoxyl, DPPH, and peroxyl radicals in this order but methionine did not. Bovine serum albumin (BSA) was less reactive toward these radicals than cysteine on molar base. Cysteine, homocysteine, and glutathione suppressed the oxidation of methyl linoleate in micelle systems, but methionine did not. The reactivity toward free radicals and antioxidant capacity of these thiol compounds were less than that of ascorbic acid, but higher than that of uric acid.

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Structure and function of heme proteins regulated by diverse post-translational modifications

Lin

2018

Archives of Biochemistry and Biophysics

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Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Cited by 9 publications

References 33 publications

Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose

Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose

Reactivity toward oxygen radicals and antioxidant action of thiol compounds

Structure and function of heme proteins regulated by diverse post-translational modifications

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