Animal ferritin and bacterioferritin contain quinones

al-Massad, F K; Kadir, Fahmi H.A.; Moore, Geoffrey R.

doi:10.1042/bj2830177

Cited by 12 publications

(5 citation statements)

References 19 publications

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“…This procedure employs heat-treatment, ammonium sulphate precipitation, ultracentrifugation and chromatography on DEAEcellulose media to purify the BFR. It is described by Al-Massad et al (1992). Protein concentrations were determined by the method of Lowry (Peterson, 1977), by using a Sigma protein assay kit (P5656) with BSA as the standard.…”

Section: Methodsmentioning

confidence: 99%

E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii

Cheesman

Kadir

Al-Basseet

et al. 1992

Biochemical Journal

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The e.p.r. and magnetic circular dichroism (m.c.d.) spectra of bacterioferritin (BFR) extracted from Pseudomonas aeruginosa and Azotobacter vinelandii have been studied over a wide temperature range down to liquid-helium temperature. The e.p.r. spectra show the presence of low-spin Fe3+ haem with g values of 2.86, 2.32, 1.48 (P. aeruginosa) and 2.88, 2.31, 1.46 (A. vinelandii), in both the presence and absence of the BFR core. Together with evidence from the porphyrin-to-Fe3+ charge-transfer band at 2240 and 2270 nm the axial haem ligands are identified as two methionines. The low-temperature m.c.d. spectra in the region 300-1000 nm of P. aeruginosa and A. vinelandii BFR are identical with one another and unaffected by removal of the iron core. Hence it can be concluded that the presence of the iron core has no detectable effect on the electronic states and on the stereochemistry of the haem group. This was unexpected, in view of the observations by Watt, Frankel, Papaefthymiou, Spartalian & Stiefel [(1986) Biochemistry 25, 4330-4336] that the redox potential of the haem group in A. vinelandii BFR shifts from -475 mV to -225 mV on removal of the core. The e.p.r. spectra of holoBFR show a broad symmetrical derivative-shaped band centred at g = 2.0 which decreases in bandwidth as the temperature is raised. This signal is assigned to the uncompensated electron spins of the iron core.

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Section: Methodsmentioning

confidence: 99%

E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii

Cheesman

Kadir

Al-Basseet

et al. 1992

Biochemical Journal

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“…( 41 , 43 , 44 ) Quinone staining by incubation with nitroblue tetrazolium in alkaline glycinate buffer has been developed and applied for the detection of quinoproteins (quinone-adducted proteins). ( 47 , 48 ) The use of a biotinylated analog combined with (strepto)avidin-labeled enzyme/beads or an analog having an azide moiety for click chemistry is another alternative. ( 9 , 19 , 40 ) Specific antibodies to quinone or quinone adduct have also been used for immunochemical detection.…”

Section: Generation Of Quinones and Reaction Toward Biomoleculesmentioning

confidence: 99%

Covalent adduction of endogenous and food-derived quinones to a protein: its biological significance

Kato

Suga

2018

J. Clin. Biochem. Nutr.

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There are many chemically reactive compounds, including quinone, in living systems and also food. Even after the ingestion of food polyphenols, quinones derived from catechol moieties could form endogenously in the body. Dopaquinone, dopamine quinone, estrogen-derived quinones, tryptamine-4,5-dione, and ubiquinone are examples of an endogenous quinone. These indicate that quinone is ubiquitously formed or present in living systems and food. Quinones can induce a variety of hazardous effects and also could have beneficial physiological effects. This review focuses on the chemical reactivity of quinone toward a biomolecule and its biological action.

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“…Many metalloproteins, all ferritins and bacterioferritins contain pyroloquinoline quinone (PPQ) or other quinonoid factors. PPQ can bind metal ions and take part in a series of protein coupled redox reactions like quinones [2,3]. Many drugs in cancer chemotherapy contain quinones [4] whereas various other uses of quinones in industry have been reported as well.…”

Section: Introductionmentioning

confidence: 99%

Derivatives of aminoquinones with N-protected amino acids

et al. 1998

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SummaryThe synthesis of derivatives of aminoquinones with N-protected amino acids is reported here. 2-Amino-1,4-benzoquinone and 2-amino-l,4-naphthoquinone, prepared by the azide method in yields of 60 and 95% respectively, were coupled with N-Boc-protected amino acids including glycine, serine, proline and tyrosine, to give the correspondening derivatives. N, NI-Diisopropylcarbodiimide/1-hydroxybenzotriazole or N, N 1-dicyclohexylcarbodiimide/HOBt used as coupling reagents provided the expected products in satisfactory yields and purities as supported by TLC, HPLC and spectral analysis.

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Animal ferritin and bacterioferritin contain quinones

Cited by 12 publications

References 19 publications

E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii

E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii

Covalent adduction of endogenous and food-derived quinones to a protein: its biological significance

Derivatives of aminoquinones with N-protected amino acids

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