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Sulfide-quinone reductase from Rhodobacter capsulatus. Purification, cloning, and expression
Year:
1997
Source of publication :
Journal of Biological Chemistry
Authors :
Shahak, Yosepha
;
.
Volume :
272
Co-Authors:
Schütz, M., Universität Regensburg, Lehrst. F. Zellbiologie P., 93040 Regensburg, Germany
Shahak, Y., Institute of Horticulture, Volcani Center, Bet-Dagan 50250, Israel
Padan, E., Hebrew University of Jerusalem, Div. Microbial Molec. Ecol., Life S., Jerusalem 91904, Israel
Hauska, G., Universität Regensburg, Lehrst. F. Zellbiologie P., 93040 Regensburg, Germany
Facilitators :
From page:
9890
To page:
9894
(
Total pages:
5
)
Abstract:
A sulfide-quinone oxidoreductase (SQR, EC 1.8.5.'.) has been purified to homogeneity from chromatophores of the non-sulfur purple bacterium Rhodobacter capsulatus DSM 155. It is composed of a single polypeptide with an apparent molecular mass of about 55 kDa, exhibiting absorption and fluorescence spectra typical for a flavoprotein and similar to the SQR from the cyanobacterium Oscillatoria limnetica. From N-terminal and tryptic peptide sequences of the pure protein a genomic DNA clone was obtained by polymerase chain reaction amplification. Its sequence contains an open reading frame of 1275 base pairs (EMBL nucleotide sequence data base, accession no. X97478) encoding the SQR of R. capsulatus. The deduced polypeptide consists of 425 amino acid residues with a molecular mass of 47 kDa and a net charge of +9. The high similarity (72%)/identity (48%) between the N termini of the cyanobacterial and the bacterial enzyme was confirmed and extended. Both enzymes exhibit the FAD/NAD(P) binding βαβ-fold (Wierenga, R. K., Terpstra, P., and Hol, W. G. S. (1986) J. Mol. Biol. 187, 101-107). The complete sequence of the SQR from R. capsulatus shows further similarity to flavoproteins, in particular glutathione reductase and lipoamide dehydrogenase. The cloned sqr was expressed in Escherichia coli in a functional form.
Note:

Registered genes:

Rhodobacter capsulatus Rbsc-2 and sqr genes, ORF2 and ORF4 DNA

Accession: X97478. GI “4581458” [GeneBank].

https://www.ncbi.nlm.nih.gov/nuccore/X97478.2?from=1&to=156

 

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More details
DOI :
10.1074/jbc.272.15.9890
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
29782
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:49
Scientific Publication
Sulfide-quinone reductase from Rhodobacter capsulatus. Purification, cloning, and expression
272
Schütz, M., Universität Regensburg, Lehrst. F. Zellbiologie P., 93040 Regensburg, Germany
Shahak, Y., Institute of Horticulture, Volcani Center, Bet-Dagan 50250, Israel
Padan, E., Hebrew University of Jerusalem, Div. Microbial Molec. Ecol., Life S., Jerusalem 91904, Israel
Hauska, G., Universität Regensburg, Lehrst. F. Zellbiologie P., 93040 Regensburg, Germany
Sulfide-quinone reductase from Rhodobacter capsulatus. Purification, cloning, and expression
A sulfide-quinone oxidoreductase (SQR, EC 1.8.5.'.) has been purified to homogeneity from chromatophores of the non-sulfur purple bacterium Rhodobacter capsulatus DSM 155. It is composed of a single polypeptide with an apparent molecular mass of about 55 kDa, exhibiting absorption and fluorescence spectra typical for a flavoprotein and similar to the SQR from the cyanobacterium Oscillatoria limnetica. From N-terminal and tryptic peptide sequences of the pure protein a genomic DNA clone was obtained by polymerase chain reaction amplification. Its sequence contains an open reading frame of 1275 base pairs (EMBL nucleotide sequence data base, accession no. X97478) encoding the SQR of R. capsulatus. The deduced polypeptide consists of 425 amino acid residues with a molecular mass of 47 kDa and a net charge of +9. The high similarity (72%)/identity (48%) between the N termini of the cyanobacterial and the bacterial enzyme was confirmed and extended. Both enzymes exhibit the FAD/NAD(P) binding βαβ-fold (Wierenga, R. K., Terpstra, P., and Hol, W. G. S. (1986) J. Mol. Biol. 187, 101-107). The complete sequence of the SQR from R. capsulatus shows further similarity to flavoproteins, in particular glutathione reductase and lipoamide dehydrogenase. The cloned sqr was expressed in Escherichia coli in a functional form.

Registered genes:

Rhodobacter capsulatus Rbsc-2 and sqr genes, ORF2 and ORF4 DNA

Accession: X97478. GI “4581458” [GeneBank].

https://www.ncbi.nlm.nih.gov/nuccore/X97478.2?from=1&to=156

 

Scientific Publication
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