Spectroscopic studies on APS reductase isolated from the hyperthermophilic sulfate-reducing archaebacterium Archaeglobus fulgidus

Jorge Lampreia; Guy Fauque; Norbert Speich; Christiane Dah1; Isabel Moura; Hans G. Truper; José J. G. Moura

doi:10.1016/S0006-291X(05)81424-X

Spectroscopic studies on APS reductase isolated from the hyperthermophilic sulfate-reducing archaebacterium Archaeglobus fulgidus

Jorge Lampreia, Guy Fauque, Norbert Speich, Christiane Dah1, Isabel Moura, Hans G. Truper, José J. G. Moura

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

Adenylyl sulfate (APS) reductase, the key enzyme of the dissimilatory sulfate respiration, catalyzes the reduction of APS (the activated form of sulfate) to sulfite with release of AMP. A spectroscopic study was carried out with the APS reductase purified from the extremely thermophilic sulfate-reducing archaebacterium Archaeoglobus fulgidus DSM 4304. Combined ultraviolet/visible spectroscopy and low temperature electron paramagnetic resonance (EPR) studies were used in order to characterize the active centers and the reactivity towards AMP and sulfite of this enzyme. The A. fulgidus APS reductase is an iron-sulfur flavoprotein containing two distinct [4Fe-4S]clusters (Centers I and II) very similar to the homologous enzyme from Desulfovibrio gigas. Center I, which has a high redox potential, is reduced by AMP and sulfite, and Center II has a very negative redox potential.

Original language	English
Pages (from-to)	342-347
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	181
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(05)81424-X
Publication status	Published - 27 Nov 1991

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title = "Spectroscopic studies on APS reductase isolated from the hyperthermophilic sulfate-reducing archaebacterium Archaeglobus fulgidus",

abstract = "Adenylyl sulfate (APS) reductase, the key enzyme of the dissimilatory sulfate respiration, catalyzes the reduction of APS (the activated form of sulfate) to sulfite with release of AMP. A spectroscopic study was carried out with the APS reductase purified from the extremely thermophilic sulfate-reducing archaebacterium Archaeoglobus fulgidus DSM 4304. Combined ultraviolet/visible spectroscopy and low temperature electron paramagnetic resonance (EPR) studies were used in order to characterize the active centers and the reactivity towards AMP and sulfite of this enzyme. The A. fulgidus APS reductase is an iron-sulfur flavoprotein containing two distinct [4Fe-4S]clusters (Centers I and II) very similar to the homologous enzyme from Desulfovibrio gigas. Center I, which has a high redox potential, is reduced by AMP and sulfite, and Center II has a very negative redox potential.",

author = "Jorge Lampreia and Guy Fauque and Norbert Speich and Christiane Dah1 and Isabel Moura and Truper, {Hans G.} and Moura, {Jos{\'e} J. G.}",

note = "Junta Nacional de Investiga{\c c}{\~a}o Cientifica and PO-LIS-FOD NATO (J. J. G. Moura) and by the Grant NTM Fr 133/20-1 of the Deutche Forchungsgeneinschafla nd by the Fonds der ChemischcnI ndustrie (H. G. Triiper).",

year = "1991",

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doi = "10.1016/S0006-291X(05)81424-X",

language = "English",

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T1 - Spectroscopic studies on APS reductase isolated from the hyperthermophilic sulfate-reducing archaebacterium Archaeglobus fulgidus

AU - Lampreia, Jorge

AU - Fauque, Guy

AU - Speich, Norbert

AU - Dah1, Christiane

AU - Moura, Isabel

AU - Truper, Hans G.

AU - Moura, José J. G.

N1 - Junta Nacional de Investigação Cientifica and PO-LIS-FOD NATO (J. J. G. Moura) and by the Grant NTM Fr 133/20-1 of the Deutche Forchungsgeneinschafla nd by the Fonds der ChemischcnI ndustrie (H. G. Triiper).

PY - 1991/11/27

Y1 - 1991/11/27

N2 - Adenylyl sulfate (APS) reductase, the key enzyme of the dissimilatory sulfate respiration, catalyzes the reduction of APS (the activated form of sulfate) to sulfite with release of AMP. A spectroscopic study was carried out with the APS reductase purified from the extremely thermophilic sulfate-reducing archaebacterium Archaeoglobus fulgidus DSM 4304. Combined ultraviolet/visible spectroscopy and low temperature electron paramagnetic resonance (EPR) studies were used in order to characterize the active centers and the reactivity towards AMP and sulfite of this enzyme. The A. fulgidus APS reductase is an iron-sulfur flavoprotein containing two distinct [4Fe-4S]clusters (Centers I and II) very similar to the homologous enzyme from Desulfovibrio gigas. Center I, which has a high redox potential, is reduced by AMP and sulfite, and Center II has a very negative redox potential.

AB - Adenylyl sulfate (APS) reductase, the key enzyme of the dissimilatory sulfate respiration, catalyzes the reduction of APS (the activated form of sulfate) to sulfite with release of AMP. A spectroscopic study was carried out with the APS reductase purified from the extremely thermophilic sulfate-reducing archaebacterium Archaeoglobus fulgidus DSM 4304. Combined ultraviolet/visible spectroscopy and low temperature electron paramagnetic resonance (EPR) studies were used in order to characterize the active centers and the reactivity towards AMP and sulfite of this enzyme. The A. fulgidus APS reductase is an iron-sulfur flavoprotein containing two distinct [4Fe-4S]clusters (Centers I and II) very similar to the homologous enzyme from Desulfovibrio gigas. Center I, which has a high redox potential, is reduced by AMP and sulfite, and Center II has a very negative redox potential.

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Spectroscopic studies on APS reductase isolated from the hyperthermophilic sulfate-reducing archaebacterium Archaeglobus fulgidus

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