An insight into phosphorylase mechanism from model study

dc.contributor.author	Tafesse F.	en
dc.contributor.author	Eguzozie K.	en
dc.date.accessioned	2012-11-01T16:31:20Z
dc.date.available	2012-11-01T16:31:20Z
dc.date.issued	2010	en
dc.identifier.citation	Synthesis and Reactivity in Inorganic, Metal-Organic and Nano-Metal Chemistry	en
dc.identifier.citation	40	en
dc.identifier.citation	10	en
dc.identifier.issn	15533174	en
dc.identifier.other	10.1080/15533174.2010.522550	en
dc.identifier.uri	http://hdl.handle.net/10500/7072
dc.description.abstract	Mechanistic aspects of phosphorylation reaction that mimic phosphorylase enzymes have been studied in the biologically important middle pH region by utilizing nitrophenol as substrate and bistrimethylenediaminecobalt(III) phosphate complexes as the enzyme model. Significant phosphorylation was noted from reactions of 1:1 molar ratio of nitrophenol and bistrimethylenediamincobalt(III) phosphate, [Co(III)tn2Pi]. Enhanced phosphorylation was depicted for reaction solutions that contained 1:1 molar ratio of nitrophenol and di-bistrimethylenediamincobalt(III) phosphate, [(Co(III)tn2)2Pi]. Specific mechanistic features and the possible roles metal ions play in phosphorylase enzyme are highlighted. Copyright © Taylor & Francis Group, LLC.	en
dc.language.iso	en	en
dc.subject	cobalt(III) complexes; enzymemodels; nitrophenol; nitrophenylphosphate; phosphorylase; phosphorylation of NP	en
dc.title	An insight into phosphorylase mechanism from model study	en
dc.type	Article	en