Sulfite:Cytochrome c Oxidoreductase fromThiobacillus novellus

Kappler, Ulrike; Bennett, Brian; Rethmeier, Jörg; Schwarz, Günter; Deutzmann, Rainer; McEwan, Alastair G.; Dahl, Christiane

doi:10.1074/jbc.275.18.13202

Cited by 159 publications

(140 citation statements)

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“…Sulfite oxidase genes, conserved in three SAGs and shared only with HTCC9565, showed more recruitment in deep water samples, and were located directly adjacent to a cytochrome in the same configuration as the sorAB genes with proven sulfite oxidase activity in Starkeya novella ATCC 8083 T (Kappler et al, 2000(Kappler et al, , 2012. The predicted AAA240-E13 sulfite oxidase had 33% identity with the S. novella SorA protein (blastp).…”

Section: )mentioning

confidence: 97%

“…The predicted AAA240-E13 sulfite oxidase had 33% identity with the S. novella SorA protein (blastp). Nearby were genes encoding for predicted Fe-S proteins, molybdopterin biosynthesis enzymes and molybdenum cofactor synthesis (Mo and heme are required cofactors (Kappler et al, 2000;Aguey-Zinsou et al, 2003)), which also appeared qualitatively more abundant in deep water samples. This may therefore indicate a mechanism for sulfur chemolithotrophy in subclade Ic and HTCC9565.…”

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confidence: 99%

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Single-cell enabled comparative genomics of a deep ocean SAR11 bathytype

et al. 2014

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Bacterioplankton of the SAR11 clade are the most abundant microorganisms in marine systems, usually representing 25% or more of the total bacterial cells in seawater worldwide. SAR11 is divided into subclades with distinct spatiotemporal distributions (ecotypes), some of which appear to be specific to deep water. Here we examine the genomic basis for deep ocean distribution of one SAR11 bathytype (depth-specific ecotype), subclade Ic. Four single-cell Ic genomes, with estimated completeness of 55%-86%, were isolated from 770 m at station ALOHA and compared with eight SAR11 surface genomes and metagenomic datasets. Subclade Ic genomes dominated metagenomic fragment recruitment below the euphotic zone. They had similar COG distributions, high local synteny and shared a large number (69%) of orthologous clusters with SAR11 surface genomes, yet were distinct at the 16S rRNA gene and amino-acid level, and formed a separate, monophyletic group in phylogenetic trees. Subclade Ic genomes were enriched in genes associated with membrane/cell wall/envelope biosynthesis and showed evidence of unique phage defenses. The majority of subclade Ic-specfic genes were hypothetical, and some were highly abundant in deep ocean metagenomic data, potentially masking mechanisms for niche differentiation. However, the evidence suggests these organisms have a similar metabolism to their surface counterparts, and that subclade Ic adaptations to the deep ocean do not involve large variations in gene content, but rather more subtle differences previously observed deep ocean genomic data, like preferential amino-acid substitutions, larger coding regions among SAR11 clade orthologs, larger intergenic regions and larger estimated average genome size.

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confidence: 97%

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confidence: 99%

Single-cell enabled comparative genomics of a deep ocean SAR11 bathytype

et al. 2014

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“…Cj0005 shows 32 % sequence identity to the wellcharacterized SorA subunit found in the chemolithotroph Starkeya novella (formerly Thiobacillus novellus). The sorAB genes of St. novella encode a periplasmic ab heterodimeric SOR, consisting of a 40?6 kDa subunit containing a molybdopterin cofactor (SorA), where sulphite oxidation takes place, and an 8?8 kDa mono-haem cytochrome c 552 (SorB) subunit which acts as a specific electron acceptor (Kappler et al, 2000. A relationship between Cj0005 and SorA was previously noted by .…”

Section: Identification Of a Putative Sor In C Jejunimentioning

confidence: 99%

“…The primary antiserum for detection of Cj0005 was kindly donated by Christiane Dahl (Institut fur Mikrobiologie und Biotechnologie, Bonn, Germany). The antiserum was prepared in rabbit and was raised against SorA of Starkeya novella, as described by Kappler et al (2000). The working concentration for this serum was a 1 : 10 000 dilution.…”

Section: Methodsmentioning

confidence: 99%

“…SOR activity was assayed by a method based on that described by Kappler et al (2000), using a Shimadzu UV-2101PC double-beam scanning spectrophotometer at a wavelength of 550 nm. Rates were obtained by measuring the increase in absorbance of cytochrome c after adding 0?5 mM sodium sulphite to a cuvette containing the following: 900 ml 10 mM Tris/HCl pH 8, 100 ml 10 mg horse heart cytochrome c ml 21 , 10-100 ml cell fraction.…”

Section: Methodsmentioning

confidence: 99%

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A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni

2005

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The ability to use sulphite as a respiratory electron donor is usually associated with free-living chemolithotrophic sulphur-oxidizing bacteria. However, this paper shows that the chemoheterotrophic human pathogen Campylobacter jejuni has the ability to respire sulphite, with oxygen uptake rates of 23±8 and 28±15 nmol O2 min−1 (mg cell protein)−1 after the addition of 0·5 mM sodium sulphite or metabisulphite, respectively, to intact cells. The C. jejuni NCTC 11168 Cj0004c and Cj0005c genes encode a monohaem cytochrome c and molybdopterin oxidoreductase, respectively, homologous to the sulphite : cytochrome c oxidoreductase (SOR) of Starkeya novella. Western blots of C. jejuni periplasm probed with a SorA antibody demonstrated cross-reaction of a 45 kDa band, consistent with the size of Cj0005. The Cj0004c gene was inactivated by insertion of a kanamycin-resistance cassette. The resulting mutant showed wild-type rates of formate-dependent respiration but was unable to respire with sulphite or metabisulphite as electron donors. 2-Heptyl-4-hydroxyquinoline-N-oxide (HQNO), a cytochrome bc 1 complex inhibitor, did not affect sulphite respiration at concentrations up to 25 μM, whereas formate respiration (which occurs partly via a bc 1 dependent route) was inhibited 50 %, thus suggesting that electrons from sulphite enter the respiratory chain after the bc 1 complex at the level of cytochrome c. Periplasmic extracts of wild-type C. jejuni 11168 showed a symmetrical absorption peak at 552 nm after the addition of sulphite, demonstrating the reduction of cytochrome c. No cytochrome c reduction was observed after addition of sulphite to periplasmic extracts of the Cj0004c mutant. A fractionation study confirmed that the majority of the SOR activity is located in the periplasm in C. jejuni, and this activity was partially purified by ion-exchange chromatography. The presence of a sulphite respiration system in C. jejuni is another example of the surprising diversity of the electron-transport chain in this small-genome pathogen. Sulphite respiration may be of importance for survival in environmental microaerobic niches and some foods, and may also provide a detoxification mechanism for this normally growth-inhibitory compound.

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Sulfite Oxidase

Kisker¹

2004

Handbook of Metalloproteins

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Sulfite oxidase catalyzes the physiologically vital oxidation of sulfite to sulfate, the terminal reaction in the oxidative degradation of the sulfur‐containing amino acids, cysteine and methionine. It belongs to the molybdenum cofactor (Moco)‐containing family of enzymes that are characterized by the presence of a mononuclear Mo atom coordinated to the sulfur atoms of a pterin derivative, named molybdopterin. The homodimeric sulfite oxidase is located in the mitochondrial intermembrane space and each subunit contains a larger Moco‐containing domain and a smaller heme‐containing domain. Oxidation of sulfite to sulfate occurs at the molybdenum center with concomitant reduction of Mo(VI) to Mo(IV). Two electrons are singly transferred to the b 5 heme of the enzyme and from there to cytochrome c . Sulfite oxidase deficiency results from defects either in the genes encoding proteins involved in molybdenum cofactor biosynthesis or in the sulfite oxidase gene itself. Several point mutations in the sulfite oxidase gene have been identified in patients with this disease worldwide. The crystal structure of wild‐type chicken sulfite oxidase provides the first atomic model for this enzyme and suggests possible reasons for how these substitutions interfere with catalysis or substrate binding.

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Sulfite:Cytochrome c Oxidoreductase fromThiobacillus novellus

Cited by 159 publications

References 63 publications

Single-cell enabled comparative genomics of a deep ocean SAR11 bathytype

Single-cell enabled comparative genomics of a deep ocean SAR11 bathytype

A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni

Sulfite Oxidase

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