Please use this identifier to cite or link to this item:
The Effect Of Dio-9 On Pyrophosphate Driven Transhydrogenation On Rhodospirillum Rubrum Chromatophores
|Title:||The Effect Of Dio-9 On Pyrophosphate Driven Transhydrogenation On Rhodospirillum Rubrum Chromatophores|
|Contributors:||Guillory, Richard (advisor)|
|Date Issued:||15 Jan 2014|
|Publisher:||University of Hawaii at Manoa|
|Abstract:||Pyrophosphatase (PPase), is an enzyme which catalyzes the hydrolysis of inorganic pyrophosphate (PPi) to organic phosphate (Pi). The relative high energy of hydrolysis (ΔG’˚) indicates that the reaction is thermodynamically irreversible. At equilibrium the reaction mixture will consist predominantly of Pi (K = 1.26 x 10-6). Many enzyme-catalyzed reactions occurring in subcellular particles produce PPi as one of their reaction products, for example ATP hydrolysis in microsomal preparation (Kennery et al, 1957) and fatty acid activation in mitochondria (Mahler, 1952) (Equation 1). In addition, PPi is formed during protein synthesis at the stage of amino acid activation (Equation 2) (Hoagland et al, 1956), during nucleic acid synthesis at the polymerization step (Kornberg, 1960) and in polysaccharide interconversion during the formation of a glycosyl donor (Leloir & Cardini, 1957).|
|Rights:||All UHM Honors Projects are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission from the copyright owner.|
|Appears in Collections:||
Honors Projects for Biology|
Please email email@example.com if you need this content in ADA-compliant format.
Items in ScholarSpace are protected by copyright, with all rights reserved, unless otherwise indicated.