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Formation of a free radical of the sulfenylimine type in the mouse ribonucleotide reductase reaction with 2'-azido-2'-deoxycytidine 5'-diphosphate
Umeå universitet.
Stockholms Universitet.
Umeå universitet.
Vise andre og tillknytning
1995 (engelsk)Inngår i: Biochimica et Biophysica Acta, Gene Structure and Expression, ISSN 0167-4781, E-ISSN 1879-2634, Vol. 1264, nr 3, s. 323-329Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Mouse and Escherichia coli ribonucleotide reductases (RR) both belong to the same class of RR, where the enzyme consists of two non-identical subunits, proteins R1 and R2. A transient free radical was observed by EPR spectroscopy in the mouse RR reaction with the suicidal inhibitor 2′-azido-2′-deoxycytidine 5′-diphosphate. The detailed hyperfine structure of the EPR spectrum of the transient radical is somewhat different for the mouse and previously studied E. coli enzymes. When the positive allosteric effector ATP was replaced by the negative effector dATP, no transient radical was observed, showing that ‘normal' binding of the inhibitor to the substrate binding site is required. Using the mouse protein R2 mutants W 103Y and D266A, where the mutations have been shown to specifically block long range electron transfer between the active site of the R1 protein to the iron/radical site in protein R2, no evidence of transient radical was found. Taken together, the data suggest that the radical is located at the active site in protein R1, and is probably of the sulfenylimine type

sted, utgiver, år, opplag, sider
1995. Vol. 1264, nr 3, s. 323-329
HSV kategori
Forskningsprogram
Biokemisk processteknik
Identifikatorer
URN: urn:nbn:se:ltu:diva-13133DOI: 10.1016/0167-4781(95)00168-9Lokal ID: c4e345e0-10b8-11df-bae5-000ea68e967bOAI: oai:DiVA.org:ltu-13133DiVA, id: diva2:986085
Merknad
Upprättat; 1995; 20100203 (ysko)Tilgjengelig fra: 2016-09-29 Laget: 2016-09-29 Sist oppdatert: 2017-11-24bibliografisk kontrollert

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