help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Originally published as Biophys J. BioFAST on June 10, 2005.
doi:10.1529/biophysj.105.059220
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow supplemental
Right arrow All Versions of this Article:
biophysj.105.059220v1
89/3/1984    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Osz, J.
Right arrow Articles by Bagyinka, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Osz, J.
Right arrow Articles by Bagyinka, C.
Biophysical Journal 89:1984-1989 (2005)
© 2005 The Biophysical Society

An Autocatalytic Step in the Reaction Cycle of Hydrogenase from Thiocapsa roseopersicina Can Explain the Special Characteristics of the Enzyme Reaction

Judit Osz and Csaba Bagyinka

Institute of Biophysics, Biological Research Center of the Hungarian Academy of Sciences, H-6701, Szeged, Hungary

Correspondence: Address reprint requests to Csaba Bagyinka, Temesvári krt. 62, Szeged, PO Box 521, H-6701, Hungary. Tel.: 36-62-599605; Fax: 36-62-433133; E-mail: csaba{at}nucleus.szbk.u-szeged.hu.

A moving front has been observed as a special pattern during the hydrogenase-catalyzed reaction of hydrogen uptake with benzyl viologen as electron acceptor in a thin-layer reaction chamber. Such fronts start spontaneously and at random times at different points of the reaction chamber; blue spheres are seen expanding at constant speed and amplitude. The number of observable starting points depends on the hydrogenase concentration. Fronts can be initiated by injecting either a small amount of completed reaction mixture or activated hydrogenase, but not by injecting a low concentration of reduced benzyl viologen. These characteristics are consistent with an autocatalytic reaction step in the enzyme reaction. The special characteristics of the hydrogen-uptake reaction in the bulk reaction (a long lag phase, and the enzyme concentration dependence of the lag phase) support the autocatalytic nature. We conclude that there is at least one autocatalytic reaction step in the hydrogenase-catalyzed reaction. The two possible autocatalytic schemes for hydrogenase are prion-type autocatalysis, in which two enzyme forms interact, and product-activation autocatalysis, where a reduced electron acceptor and an inactive enzyme form interact. The experimental results strongly support the occurrence of prion-type autocatalysis.




This article has been cited by other articles:


Home page
Biophys. JHome page
J. Osz, G. Bodo, R. M. M. Branca, and C. Bagyinka
Theoretical Calculations on Hydrogenase Kinetics: Explanation of the Lag Phase and the Enzyme Concentration Dependence of the Activity of Hydrogenase Uptake
Biophys. J., September 1, 2005; 89(3): 1957 - 1964.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2005 by the Biophysical Society.