Hydrogen Enhances Nickel Tolerance in the Purple Sulfur Bacterium Thiocapsa roseopersicina

2010 ◽  
Vol 44 (2) ◽  
pp. 834-840 ◽  
Author(s):  
Oleg A. Zadvornyy ◽  
Mark Allen ◽  
Susan K. Brumfield ◽  
Zack Varpness ◽  
Eric S. Boyd ◽  
...  
Keyword(s):  
Purple Sulfur Bacterium ◽  
Nickel Tolerance ◽  
Thiocapsa Roseopersicina

Growth and metabolism of the purple sulfur bacterium Thiocapsa roseopersicina under combined light/dark and oxic/anoxic regimens

1990 ◽  
Vol 154 (5) ◽  
pp. 459-464 ◽  
Author(s):  
Rutger de Wit ◽  
Hans van Gemerden
Keyword(s):  
Purple Sulfur Bacterium ◽  
Thiocapsa Roseopersicina

scholarly journals Cyanobacterial-Type, Heteropentameric, NAD+-Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina

2004 ◽  
Vol 70 (2) ◽  
pp. 722-728 ◽  
Author(s):  
Gábor Rákhely ◽  
Ákos T. Kovács ◽  
Gergely Maróti ◽  
Barna D. Fodor ◽  
Gyula Csanádi ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Photosynthetic Bacterium ◽  
Hydrogenase Activity ◽  
Structural Genes ◽  
Purple Sulfur Bacterium ◽  
Thiocapsa Roseopersicina ◽  
Reverse Transcription Pcr ◽  
Single Transcript

ABSTRACT Structural genes coding for two membrane-associated NiFe hydrogenases in the phototrophic purple sulfur bacterium Thiocapsa roseopersicina (hupSL and hynSL) have recently been isolated and characterized. Deletion of both hydrogenase structural genes did not eliminate hydrogenase activity in the cells, and considerable hydrogenase activity was detected in the soluble fraction. The enzyme responsible for this activity was partially purified, and the gene cluster coding for a cytoplasmic, NAD+-reducing NiFe hydrogenase was identified and sequenced. The deduced gene products exhibited the highest similarity to the corresponding subunits of the cyanobacterial bidirectional soluble hydrogenases (HoxEFUYH). The five genes were localized on a single transcript according to reverse transcription-PCR experiments. A σ54-type promoter preceded the gene cluster, suggesting that there was inducible expression of the operon. The Hox hydrogenase was proven to function as a truly bidirectional hydrogenase; it produced H2 under nitrogenase-repressed conditions, and it recycled the hydrogen produced by the nitrogenase in cells fixing N2. In-frame deletion of the hoxE gene eliminated hydrogen evolution derived from the Hox enzyme in vivo, although it had no effect on the hydrogenase activity in vitro. This suggests that HoxE has a hydrogenase-related role; it likely participates in the electron transfer processes. This is the first example of the presence of a cyanobacterial-type, NAD+-reducing hydrogenase in a phototrophic bacterium that is not a cyanobacterium. The potential physiological implications are discussed.

scholarly journals HupO, a Novel Regulator Involved in Thiosulfate-Responsive Control of HupSL [NiFe]-Hydrogenase Synthesis in Thiocapsa roseopersicina

2016 ◽  
Vol 82 (7) ◽  
pp. 2039-2049 ◽  
Author(s):  
Ildikó K. Nagy ◽  
Kornél L. Kovács ◽  
Gábor Rákhely ◽  
Gergely Maróti
Keyword(s):  
Transcriptional Repression ◽  
Rhodobacter Capsulatus ◽  
Sulfur Metabolism ◽  
Enzyme Synthesis ◽  
Regulatory Control ◽  
Bacterial Cells ◽  
Purple Sulfur Bacterium ◽  
Content Type ◽  
Thiocapsa Roseopersicina

ABSTRACT[NiFe]-hydrogenases are regulated by various factors to fulfill their physiological functions in bacterial cells. The photosynthetic purple sulfur bacteriumThiocapsa roseopersicinaharbors four functional [NiFe]-hydrogenases: HynSL, HupSL, Hox1, and Hox2. Most of these hydrogenases are functionally linked to sulfur metabolism, and thiosulfate has a central role in this organism. The membrane-associated Hup hydrogenases have been shown to play a role in energy conservation through hydrogen recycling. The expression of Hup-type hydrogenases is regulated by H2inRhodobacter capsulatusandCupriavidus necator; however, it has been shown that the corresponding hydrogen-sensing system is nonfunctional inT. roseopersicinaand that thiosulfate is a regulating factor ofhupexpression. Here, we describe the discovery and analysis of mutants of a putative regulator (HupO) of the Hup hydrogenase inT. roseopersicina. HupO appears to mediate the transcriptional repression of Hup enzyme synthesis under low-thiosulfate conditions. We also demonstrate that the presence of the Hox1 hydrogenase strongly influences Hup enzyme synthesis in thathupexpression was decreased significantly in thehox1mutant. This reduction in Hup synthesis could be reversed by mutation ofhupO, which resulted in strongly elevatedhupexpression, as well as Hup protein levels, and concomitantin vivohydrogen uptake activity in thehox1mutant. However, this regulatory control was observed only at low thiosulfate concentrations. Additionally, weak hydrogen-dependenthupexpression was shown in thehupOmutant strain lacking the Hox1 hydrogenase. HupO-mediated Hup regulation therefore appears to link thiosulfate metabolism and the hydrogenase network inT. roseopersicina.

Induced mutagenesis by bleomycin in the purple sulfur bacterium Thiocapsa roseopersicina

1995 ◽  
Vol 30 (2) ◽  
pp. 117-120 ◽  
Author(s):  
Victoria Pav�n ◽  
Isabel Esteve ◽  
Ricardo Guerrero ◽  
Antonio Villaverde ◽  
N�ria Gaju
Keyword(s):  
Purple Sulfur Bacterium ◽  
Thiocapsa Roseopersicina ◽  
Induced Mutagenesis

scholarly journals Turnover of dimethylsulfoniopropionate (DMSP) by the purple sulfur bacterium Thiocapsa roseopersicina M11: ecological implications

1998 ◽  
Vol 27 (3) ◽  
pp. 281-290 ◽  
Author(s):  
Henk M Jonkers ◽  
Saskia Bruin ◽  
Hans Gemerden
Keyword(s):  
Purple Sulfur Bacterium ◽  
Thiocapsa Roseopersicina ◽  
Ecological Implications

A High Potential Iron Sulfur Protein of the Purple Sulfur Bacterium Thiocapsa roseopersicina

1980 ◽  
Vol 35 (1-2) ◽  
pp. 150-153 ◽  
Author(s):  
Ulrich Fischer
Keyword(s):  
Heme Iron ◽  
High Potential ◽  
Reduced Form ◽  
Sephadex Column ◽  
Purple Sulfur Bacterium ◽  
Thiocapsa Roseopersicina ◽  
Non Heme Iron ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

Abstract Thiocapsa roseopersicina, High Potential Iron Sulfur Pro­ tein (HIPIP), Phototrophic Bacteria High potential iron sulfur protein (HIPIP) from the purple sulfur bacterium Thiocapsa roseopersicina was isolated in the oxidized and reduced form by DEAE-and Sephadex column chromatography (best purity index A 282 nm red/A 385 nm red. = 3.78). The enzyme contains non-heme iron and acid-labile sulfide in an equimolar ratio. The enzyme shows no aconitase activity.

Photofermentative production of hydrogen from organic acids by the purple sulfur bacterium Thiocapsa roseopersicina

2013 ◽  
Vol 38 (14) ◽  
pp. 5535-5544 ◽  
Author(s):  
Andrea Nyilasi ◽  
Éva Molnos ◽  
Szabolcs Lányi ◽  
Iosif Nagy ◽  
Gábor Rákhely ◽  
...  
Keyword(s):  
Organic Acids ◽  
Purple Sulfur Bacterium ◽  
Thiocapsa Roseopersicina ◽  
Production Of Hydrogen
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