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<Emphasis Type="Italic">Rhodobacter capsulatus</Emphasis> porphobilinogen synthase,a high activity metal ion independent hexamer
Authors:Email author" target="_blank">David?W?BollivarEmail author  Cheryl?Clauson  Rachel?Lighthall  Siiri?Forbes  Bashkim?Kokona  Robert?Fairman  Lenka?Kundrat  Eileen?K?Jaffe
Institution:(1) Department of Biology, Illinois Wesleyan University, P.O. Box 2900, Bloomington, IL 61702-2900, USA;(2) Biology Department, Haverford College, Haverford, PA 19041, USA;(3) Fox Chase Cancer Center, 333 Cottman Avenue, Philadelphia, PA 19111, USA
Abstract:

Background  

The enzyme porphobilinogen synthase (PBGS), which is central to the biosynthesis of heme, chlorophyll and cobalamins, has long been known to use a variety of metal ions and has recently been shown able to exist in two very different quaternary forms that are related to metal ion usage. This paper reports new information on the metal ion independence and quaternary structure of PBGS from the photosynthetic bacterium Rhodobacter capsulatus.
Keywords:
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