Research Collection. Human Cu,Zn-superoxide dismutase preparation of the apo-protein. Calorimetriy and pulse radiolysis. Doctoral Thesis.
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1 Research Collection Doctoral Thesis Human Cu,Zn-superoxide dismutase preparation of the apo-protein. Calorimetriy and pulse radiolysis Author(s): Sutter, Barbara Publication Date: 2000 Permanent Link: Rights / License: In Copyright - Non-Commercial Use Permitted This page was generated automatically upon download from the ETH Zurich Research Collection. For more information please consult the Terms of use. ETH Library
2 Diss. ETH Nr Human Cu,Zn-Superoxide Dismutase: Preparation of the apo-protein. Calorimetry and Pulse Radiolysis. A Dissertation submitted to the FEDERAL INSTITUTE OF TECHNOLOGY for the Degree of DOCTOR OF NATURAL SCIENCES presented by BARBARA SUTTER DipL Chem. ETH born of Hemmiken BL Accepted on the recommendation of: Prof. Dr. Willem H. Koppenol, Examiner Prof. Dr. Ursula Räthlisberger, Co-Examiner 2000
3 Abstract The superoxide dismutases (EC ) are a family of enzymes that catalyse the dismutation of superoxide radical anion to dioxygen and hydrogen peroxide. The active site contains a redox-active metal ion such as manganese, iron, or copper. The copper-containing protein has also one zinc ion bound per subunit. The standard method to remove the metal ions from CU,Zn superoxide dismutase has been to exhaustively dialyse the protein against chelating agents at low ph. A new method was developed where the protein is bound to ion exchange medium based on iminodiacetic acid immobilized on Sepharose. Results are shown for both human and bovine dimeric CU,Zn superoxide dismutase and the monomeric Escherichia coli CU,Zn superoxide dismutase. In every case, the metals were removed efficiently. Abstract
4 ii The human apo-protein was then used for studies of the metal binding properties by isothermal titration ealorimetry. Binding eonstants as weh as enthalpies were determined in a single experiment, ahowing for a eomplete thermodynamie eharaeterisation of the system. At ph 7.3, the stability eonstants obtained for the binding of metal ions to their native sites eorrespond with values found in the literature. The two binding sites on one subunit are interacting at this ph. For the binding of zine ions to apo protein, a site binding eonstant of (8.6±0.9)10 16 was determined and for the eopper binding to the apo protein this value is (4±2)10 18 at 25 C in 1-methylimidazole buffer. Aetivity of the reeonstituted protein was analysed by pulse radiolysis. For protein reeonstituted with two equivalents ofboth zine and eopper, the rate eonstant was (1.09±0.04)10 9 M-Is-I, for protein reeonstituted with four equivalents of eopper (8.4±0.9)10 8 M-Is- I and for protein reeonstituted only with two equivalents of eopper (3.5±0.5)10 8 M-Is- I. At ph 5.0, the binding properties are entirely different; while eopper ions are bound to all four binding sites with a site binding eonstant of (2±1)10 6, zine binds only to one set oftwo binding sites with a site binding eonstant of (4±2)10 7. Abstract
5 iii Zusammenfassung Superoxid Dismutasen (EC ) sind eine Familie von Enzymen, die die Dismutierung von Superoxid Radikalen zu Wasserstoffperoxid und Sauerstoff katalysieren. Die aktive Stelle beinhaltet redox-aktive Metallionen wie Mangan, Eisen oder Kupfer. Im kupferhaltigen Enzym ist zudem ein Zinkion pro Untereinheit gebunden. Nach der Standardmethode werden Metallionen aus CU,Zn Superoxid Dismutase entfernt indem man das Protein längere Zeit bei tiefem pr-wert gegen Chelatliganden dialysiert. Eine neuartige Methode wurde entwickelt, bei der das Protein an ein Ionen-Austausch-Medium gebunden wird, das aus an Sepharose gebundener Iminodiessigsäure besteht. Dies wurde sowohl für menschliche Superoxid Dismutase wie auch für das Rinderenzym sowie das monomere Protein aus Escherichia coligetestet. In allen Fällen wurden die Metallionen gründlich entfernt. Zusammenfassung
6 iv Das menschliche Protein wurde dann für Studien der Metallbindungseigenschaften durch isothermale Titrationskalorimetrie benutzt. Diese Methode ermöglicht sowohl die Bestimmung von Stabilitätskonstanten wie auch von Enthalpien In einem einzagen Experiment, was die vollständige thermodynamische Charakterisierung des Systems erlaubt. Bei ph 7.3 entsprechen die erhaltenen Stabilitätskonstanten den aus der Literatur bekannten. Bei diesem ph-wert gibt es eine Wechselwirkung zwischen den Bindungsstellen auf einer Untereinheit. Die spezifische Bindungskonstante für die Bindung von Zink an apo Superoxid Dismutase beträgt (8.6±0.9)10 16, diejenige für Kupfer (4±2)10 18 bei 25 C in l-methylimidazolat Puffer. Die enzymatische Aktivität der wieder hergestellten Proteine wurde mittels Pulsradiolyse bestimmt. Für Protein, dem Kupfer und Zink zugegeben wurde, beträgt die Geschwindigkeitskonstante (1.09±0.04)10 9 M-Is- I; wenn vier Äquivalente Kupfer zugegeben wurden (8.4±0.9)10 8 M-Is- I und nach der Zugabe von nur zwei Äquivalenten Kupfer (3.5±0.5)10 8 M-Is I. Bei ph 5.0 waren die Stabilitätskonstanten ganz verschieden. Kupferionen weisen für beide Bindungsstellen ähnliche Eigenschaften auf mit einer spezifischen Bindungskonstanten von (2±1)10 6, während Zinkionen nur an eine Bindungsstelle gebunden werden mit einer spezifischen Bindungskonstanten von (4±2)10 7. Zusammenfassung
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