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Design and synthesis of water soluble (metallo)porphyrins with pendant arms: studies of binding to xanthine oxidase

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Design and synthesis of water soluble (metallo)porphyrins with pendant arms: studies of binding to xanthine oxidase. / Gibson, Elizabeth A.; Duhme-Klair, Anne-K; Perutz, Robin N.

In: NEW JOURNAL OF CHEMISTRY, Vol. 34, No. 6, 2010, p. 1125-1134.

Research output: Contribution to journalArticle

Harvard

Gibson, EA, Duhme-Klair, A-K & Perutz, RN 2010, 'Design and synthesis of water soluble (metallo)porphyrins with pendant arms: studies of binding to xanthine oxidase', NEW JOURNAL OF CHEMISTRY, vol. 34, no. 6, pp. 1125-1134. https://doi.org/10.1039/b9nj00736a

APA

Gibson, E. A., Duhme-Klair, A-K., & Perutz, R. N. (2010). Design and synthesis of water soluble (metallo)porphyrins with pendant arms: studies of binding to xanthine oxidase. NEW JOURNAL OF CHEMISTRY, 34(6), 1125-1134. https://doi.org/10.1039/b9nj00736a

Vancouver

Gibson EA, Duhme-Klair A-K, Perutz RN. Design and synthesis of water soluble (metallo)porphyrins with pendant arms: studies of binding to xanthine oxidase. NEW JOURNAL OF CHEMISTRY. 2010;34(6):1125-1134. https://doi.org/10.1039/b9nj00736a

Author

Gibson, Elizabeth A. ; Duhme-Klair, Anne-K ; Perutz, Robin N. / Design and synthesis of water soluble (metallo)porphyrins with pendant arms: studies of binding to xanthine oxidase. In: NEW JOURNAL OF CHEMISTRY. 2010 ; Vol. 34, No. 6. pp. 1125-1134.

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@article{469444ddcceb43db9ac871cf6593b36b,
title = "Design and synthesis of water soluble (metallo)porphyrins with pendant arms: studies of binding to xanthine oxidase",
abstract = "The tethering of a substrate analogue to a covalently attached luminophore may give rise to a probe for reporting enzyme activity spectrofluorometrically. The overall design incorporates a water-soluble porphyrin luminophore, a substrate analogue and a planar conjugated bridge of the appropriate length designed to bind in the substrate-access channel of xanthine oxidase (XO). 5,10,15-Tris(N-methyl-4-pyridiniumyl)-20-phenyl porphyrins was functionalised at the 4-position of the phenyl group with amide-linked 2-methoxy-benzamide groups, [(2-methoxy-4-aminophenylcarbonyl)amino] or [(2-methoxy-4-[(pyridine-4-carbonyl)-amino]-phenylcarbonyl)-amino]. The products were isolated as free base or zinc porphyrins with chloride or hexafluorophosphate counterions and characterised by optical emission and absorption in addition to other spectroscopic methods. Binding studies of bovine XO to the zinc porphyrin trichloride derivatives with the above linkers were used to determine the IC50 of 81 and 113 mu M and K-i values of 4.6 and 6.5 mu M, respectively. Furthermore, addition of XO to an aqueous solution of the products caused quenching of the porphyrin emission and a red shift in the absorption spectrum.",
keywords = "DEHYDROGENASE, MECHANISM, METAL, CONVERSION, COMPLEXES, SWITCHES, SENSORS, ENZYMES",
author = "Gibson, {Elizabeth A.} and Anne-K Duhme-Klair and Perutz, {Robin N.}",
year = "2010",
doi = "10.1039/b9nj00736a",
language = "English",
volume = "34",
pages = "1125--1134",
journal = "NEW JOURNAL OF CHEMISTRY",
issn = "1144-0546",
publisher = "Royal Society of Chemistry",
number = "6",

}

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TY - JOUR

T1 - Design and synthesis of water soluble (metallo)porphyrins with pendant arms: studies of binding to xanthine oxidase

AU - Gibson, Elizabeth A.

AU - Duhme-Klair, Anne-K

AU - Perutz, Robin N.

PY - 2010

Y1 - 2010

N2 - The tethering of a substrate analogue to a covalently attached luminophore may give rise to a probe for reporting enzyme activity spectrofluorometrically. The overall design incorporates a water-soluble porphyrin luminophore, a substrate analogue and a planar conjugated bridge of the appropriate length designed to bind in the substrate-access channel of xanthine oxidase (XO). 5,10,15-Tris(N-methyl-4-pyridiniumyl)-20-phenyl porphyrins was functionalised at the 4-position of the phenyl group with amide-linked 2-methoxy-benzamide groups, [(2-methoxy-4-aminophenylcarbonyl)amino] or [(2-methoxy-4-[(pyridine-4-carbonyl)-amino]-phenylcarbonyl)-amino]. The products were isolated as free base or zinc porphyrins with chloride or hexafluorophosphate counterions and characterised by optical emission and absorption in addition to other spectroscopic methods. Binding studies of bovine XO to the zinc porphyrin trichloride derivatives with the above linkers were used to determine the IC50 of 81 and 113 mu M and K-i values of 4.6 and 6.5 mu M, respectively. Furthermore, addition of XO to an aqueous solution of the products caused quenching of the porphyrin emission and a red shift in the absorption spectrum.

AB - The tethering of a substrate analogue to a covalently attached luminophore may give rise to a probe for reporting enzyme activity spectrofluorometrically. The overall design incorporates a water-soluble porphyrin luminophore, a substrate analogue and a planar conjugated bridge of the appropriate length designed to bind in the substrate-access channel of xanthine oxidase (XO). 5,10,15-Tris(N-methyl-4-pyridiniumyl)-20-phenyl porphyrins was functionalised at the 4-position of the phenyl group with amide-linked 2-methoxy-benzamide groups, [(2-methoxy-4-aminophenylcarbonyl)amino] or [(2-methoxy-4-[(pyridine-4-carbonyl)-amino]-phenylcarbonyl)-amino]. The products were isolated as free base or zinc porphyrins with chloride or hexafluorophosphate counterions and characterised by optical emission and absorption in addition to other spectroscopic methods. Binding studies of bovine XO to the zinc porphyrin trichloride derivatives with the above linkers were used to determine the IC50 of 81 and 113 mu M and K-i values of 4.6 and 6.5 mu M, respectively. Furthermore, addition of XO to an aqueous solution of the products caused quenching of the porphyrin emission and a red shift in the absorption spectrum.

KW - DEHYDROGENASE

KW - MECHANISM

KW - METAL

KW - CONVERSION

KW - COMPLEXES

KW - SWITCHES

KW - SENSORS

KW - ENZYMES

UR - http://www.scopus.com/inward/record.url?scp=77953155678&partnerID=8YFLogxK

U2 - 10.1039/b9nj00736a

DO - 10.1039/b9nj00736a

M3 - Article

VL - 34

SP - 1125

EP - 1134

JO - NEW JOURNAL OF CHEMISTRY

JF - NEW JOURNAL OF CHEMISTRY

SN - 1144-0546

IS - 6

ER -