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Hydride-transfer transition structure as a possible unifying redox step for describing the branched mechanism of glutathione reductase. Molecular-electronic antecedents
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry.
2000 (English)In: THEORETICAL CHEMISTRY ACCOUNTS, ISSN 1432-881X, Vol. 103, no 6, 451-462 p.Article in journal (Refereed) Published
Abstract [en]

For glutathione reductase (GR), a mammalian reduced nicotinamide adenine dinucleotide phosphate dependent flavoenzyme participating in free-radical detoxification pathways, we present a quantum chemical study addressing aspects of its electronic mechanism

Place, publisher, year, edition, pages
SPRINGER VERLAG , 2000. Vol. 103, no 6, 451-462 p.
Keyword [en]
branched mechanism; glutathione reductase; catalytic mechanism; transposed hydride transfer; proton relays; CATALYTIC MECHANISM; ENZYME; RESOLUTION; BINDING; MODELS; FLAVINS; SITE; SCF; OLD
URN: urn:nbn:se:uu:diva-36990OAI: oai:DiVA.org:uu-36990DiVA: diva2:64889
Addresses: Tapia O, Univ Uppsala, Dept Phys Chem, Box 532, S-75121 Uppsala, Sweden. Univ Uppsala, Dept Phys Chem, S-75121 Uppsala, Sweden. Univ Republ, Fac Quim, Catedra Quim Cuant, Montevideo 11800, Uruguay.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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