The autocatalytic step is an integral part of the hydrogenase cycle

Sarolta Bankó, Zsuzsanna Kucsma, G. Lente, Csaba Bagyinka

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

We earlier proved the involvement of an autocatalytic step in the oxidation of H2 by HynSL hydrogenase from Thiocapsa roseopersicina, and demonstrated that two enzyme forms interact in this step. Using a modified thin-layer reaction chamber which permits quantitative analysis of the concentration of the reaction product (reduced benzyl viologen) in the reaction volume during the oxidation of H2, we now show that the steady-state concentration of the product displays a strong enzyme concentration dependence. This experimental fact can be explained only if the previously detected autocatalytic step occurs inside the catalytic enzyme-cycle and not in the enzyme activation process. Consequently, both interacting enzyme forms should participate in the catalytic cycle of the enzyme. As far as we are aware, this is the first experimental observation of such a phenomenon resulting in an apparent inhibition of the enzyme. It is additionally concluded that the interaction of the two enzyme forms should result in a conformational change in the enzyme-substrate form. This scheme is very similar to that of prion reactions. Since merely a few molecules are involved at some point of the reaction, this process is entirely stochastic in nature. We have therefore developed a stochastic calculation method, calculations with which lent support to the conclusion drawn from the experiment.

Original languageEnglish
Pages (from-to)658-664
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1834
Issue number3
DOIs
Publication statusPublished - Mar 2013

Fingerprint

Hydrogenase
Enzymes
Thiocapsa roseopersicina
Benzyl Viologen
Enzyme Activation
Prions
Oxidation
Reaction products
Observation
Chemical activation
Molecules

Keywords

  • Autocatalysis
  • Autocatalytic enzyme reaction
  • Autocatalytic extinction
  • Enzyme kinetics
  • Hydrogenase
  • Kinetic model

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Analytical Chemistry
  • Molecular Biology

Cite this

The autocatalytic step is an integral part of the hydrogenase cycle. / Bankó, Sarolta; Kucsma, Zsuzsanna; Lente, G.; Bagyinka, Csaba.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1834, No. 3, 03.2013, p. 658-664.

Research output: Contribution to journalArticle

Bankó, Sarolta ; Kucsma, Zsuzsanna ; Lente, G. ; Bagyinka, Csaba. / The autocatalytic step is an integral part of the hydrogenase cycle. In: Biochimica et Biophysica Acta - Proteins and Proteomics. 2013 ; Vol. 1834, No. 3. pp. 658-664.
@article{aa5405f44586475d846ddbb156c29cf1,
title = "The autocatalytic step is an integral part of the hydrogenase cycle",
abstract = "We earlier proved the involvement of an autocatalytic step in the oxidation of H2 by HynSL hydrogenase from Thiocapsa roseopersicina, and demonstrated that two enzyme forms interact in this step. Using a modified thin-layer reaction chamber which permits quantitative analysis of the concentration of the reaction product (reduced benzyl viologen) in the reaction volume during the oxidation of H2, we now show that the steady-state concentration of the product displays a strong enzyme concentration dependence. This experimental fact can be explained only if the previously detected autocatalytic step occurs inside the catalytic enzyme-cycle and not in the enzyme activation process. Consequently, both interacting enzyme forms should participate in the catalytic cycle of the enzyme. As far as we are aware, this is the first experimental observation of such a phenomenon resulting in an apparent inhibition of the enzyme. It is additionally concluded that the interaction of the two enzyme forms should result in a conformational change in the enzyme-substrate form. This scheme is very similar to that of prion reactions. Since merely a few molecules are involved at some point of the reaction, this process is entirely stochastic in nature. We have therefore developed a stochastic calculation method, calculations with which lent support to the conclusion drawn from the experiment.",
keywords = "Autocatalysis, Autocatalytic enzyme reaction, Autocatalytic extinction, Enzyme kinetics, Hydrogenase, Kinetic model",
author = "Sarolta Bank{\'o} and Zsuzsanna Kucsma and G. Lente and Csaba Bagyinka",
year = "2013",
month = "3",
doi = "10.1016/j.bbapap.2012.12.018",
language = "English",
volume = "1834",
pages = "658--664",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - The autocatalytic step is an integral part of the hydrogenase cycle

AU - Bankó, Sarolta

AU - Kucsma, Zsuzsanna

AU - Lente, G.

AU - Bagyinka, Csaba

PY - 2013/3

Y1 - 2013/3

N2 - We earlier proved the involvement of an autocatalytic step in the oxidation of H2 by HynSL hydrogenase from Thiocapsa roseopersicina, and demonstrated that two enzyme forms interact in this step. Using a modified thin-layer reaction chamber which permits quantitative analysis of the concentration of the reaction product (reduced benzyl viologen) in the reaction volume during the oxidation of H2, we now show that the steady-state concentration of the product displays a strong enzyme concentration dependence. This experimental fact can be explained only if the previously detected autocatalytic step occurs inside the catalytic enzyme-cycle and not in the enzyme activation process. Consequently, both interacting enzyme forms should participate in the catalytic cycle of the enzyme. As far as we are aware, this is the first experimental observation of such a phenomenon resulting in an apparent inhibition of the enzyme. It is additionally concluded that the interaction of the two enzyme forms should result in a conformational change in the enzyme-substrate form. This scheme is very similar to that of prion reactions. Since merely a few molecules are involved at some point of the reaction, this process is entirely stochastic in nature. We have therefore developed a stochastic calculation method, calculations with which lent support to the conclusion drawn from the experiment.

AB - We earlier proved the involvement of an autocatalytic step in the oxidation of H2 by HynSL hydrogenase from Thiocapsa roseopersicina, and demonstrated that two enzyme forms interact in this step. Using a modified thin-layer reaction chamber which permits quantitative analysis of the concentration of the reaction product (reduced benzyl viologen) in the reaction volume during the oxidation of H2, we now show that the steady-state concentration of the product displays a strong enzyme concentration dependence. This experimental fact can be explained only if the previously detected autocatalytic step occurs inside the catalytic enzyme-cycle and not in the enzyme activation process. Consequently, both interacting enzyme forms should participate in the catalytic cycle of the enzyme. As far as we are aware, this is the first experimental observation of such a phenomenon resulting in an apparent inhibition of the enzyme. It is additionally concluded that the interaction of the two enzyme forms should result in a conformational change in the enzyme-substrate form. This scheme is very similar to that of prion reactions. Since merely a few molecules are involved at some point of the reaction, this process is entirely stochastic in nature. We have therefore developed a stochastic calculation method, calculations with which lent support to the conclusion drawn from the experiment.

KW - Autocatalysis

KW - Autocatalytic enzyme reaction

KW - Autocatalytic extinction

KW - Enzyme kinetics

KW - Hydrogenase

KW - Kinetic model

UR - http://www.scopus.com/inward/record.url?scp=84873030154&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84873030154&partnerID=8YFLogxK

U2 - 10.1016/j.bbapap.2012.12.018

DO - 10.1016/j.bbapap.2012.12.018

M3 - Article

VL - 1834

SP - 658

EP - 664

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 3

ER -