Auracyanin, a blue copper protein from the green photosynthetic bacterium Chloroflexus aurantiacus

Trost, Jeffrey T.; McManus, James D.; Freeman, John; Ramakrishna, B. L.; Blankenship, Robert E.

doi:10.1021/bi00420a041

Cited by 44 publications

(6 citation statements)

References 39 publications

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“…The possible explanation for this behaviour is that loss of the copper atom from the denatured protein permits the single-cysteine-residue thiol group, which in native pseudoazurin is a ligand to the copper, to form an S-S bridge to a second polypeptide chain. A similar phenomenon has recently been reported for amicyanin from P. denitrificans [22] and may account for the dimeric forms of other blue copper proteins, including auracyanins from Chloroflesus auranticans [5,23] and halocyanin from Natronobacterium pharaonis [24] observed under certain conditions.…”

Section: Discussionsupporting

confidence: 77%

The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha

Chan

Willis

Robinson

et al. 1995

Biochemical Journal

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The complete amino acid sequence, obtained by direct protein sequencing, of the pseudoazurin from Thiosphaera pantotropha is reported. It shows sequence identities varying from 46 to 66% with previously sequenced pseudoazurins. Previously identified conserved residues with key functions in pseudoazurins are found in the protein from T. pantotropha with the exception of glycine-39, the carbonyl group of which has been considered as a ligand to the copper, which is replaced by a serine residue. Electrospray-ionization MS (ESI-MS) has shown that pseudoazurin from T. pantotropha often contains two polypeptide species differing in molecular mass by 16 Da, presumably owing to oxidation of a methionine residue to a sulphoxide derivative. These two species have different endoproteinase Arg-C digestion patterns. Conditions for ESI-MS were identified that permitted either the retention or the loss of the single copper ion associated with the pseudoazurin. The aberrant tendency of T. pantotropha pseudoazurin to form a disulphide-bridged dimer on SDS/PAGE under some conditions is described.

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Section: Discussionsupporting

confidence: 77%

The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha

Chan

Willis

Robinson

et al. 1995

Biochemical Journal

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“…According to 16S rRNA analysis, it is the earliest branching organism within the eubacteria that exhibits the photosynthetic phenotype (Woese 1987). In addition to the reaction center traits discussed earlier, this organism has many decidedly unusual features, including a novel pathway of carbon fixation (neither the Calvin cycle nor the reverse TCA cycle) (Holo and Sirevhg 1986), an unusual lipid 99 and carotenoid composition (Knudsen et al 1982), an apparent lack of soluble c-type cytochromes (Bartsch 1978, Freeman andBlankenship 1990) (the blue copper protein known as auracyanin (Trost et al 1988, McManus et al 1992 probably fulfills their functional role), novel amino acid biosynthetic pathways (Klemme 1989) and finally a cell wall structure that is very atypical for a Gram negative organism (Jurgens et al 1987). In overall cell morphology, carotenoid composition and mat-forming behavior, it is similar to certain types of cyanobacteria (Pierson and Castenholz 1974a,b).…”

Section: The Special Position Of Chloroflexus Aurantiacusmentioning

confidence: 98%

Origin and early evolution of photosynthesis

1992

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Photosynthesis was well-established on the earth at least 3.5 thousand million years ago, and it is widely believed that these ancient organisms had similar metabolic capabilities to modern cyanobacteria. This requires that development of two photosystems and the oxygen evolution capability occurred very early in the earth's history, and that a presumed phase of evolution involving non-oxygen evolving photosynthetic organisms took place even earlier. The evolutionary relationships of the reaction center complexes found in all the classes of currently existing organisms have been analyzed using sequence analysis and biophysical measurements. The results indicate that all reaction centers fall into two basic groups, those with pheophytin and a pair of quinones as early acceptors, and those with iron sulfur clusters as early acceptors. No simple linear branching evolutionary scheme can account for the distribution patterns of reaction centers in existing photosynthetic organisms, and lateral transfer of genetic information is considered as a likely possibility. Possible scenarios for the development of primitive reaction centers into the heterodimeric protein structures found in existing reaction centers and for the development of organisms with two linked photosystems are presented.

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“…2011 ). It has been proposed that the electrons from this complex reduce auracyanin, a blue-copper protein serving as mobile electron carrier from ACIII to the RC, where it could act as an electron donor for the cytochrome c ( Trost et al. 1988 ; McManus et al.…”

Section: Resultsmentioning

confidence: 99%

A Novel Microbialite-Associated Phototrophic Chloroflexi Lineage Exhibiting a Quasi-Clonal Pattern along Depth

Saghaï

Zivanovic

Moreira

et al. 2020

Genome Biology and Evolution

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Chloroflexales (Chloroflexi) are typical members of the anoxygenic photosynthesizing component of microbial mats and have mostly been characterized from communities associated to hot springs. Here, we report the assembly of five metagenome-assembled genomes of a novel lineage of Chloroflexales found in mesophilic lithifying microbial mats (microbialites) in Lake Alchichica (Mexico). Genomic and phylogenetic analyses revealed that the bins shared 92% of their genes, and these genes were nearly identical despite being assembled from samples collected along a depth gradient (1-15 m depth). We tentatively name this lineage Candidatus Lithoflexus mexicanus. Metabolic predictions based on the MAGs suggest that these chlorosome-lacking mixotrophs share features in central carbon metabolism, electron transport, as well as adaptations to life under oxic and anoxic conditions, with members of two related lineages, Chloroflexineae and Roseiflexineae. Contrasting with the other diverse microbialite community members, which display much lower genomic conservation along the depth gradient, Ca. L. mexicanus MAGs exhibit remarkable similarity. This might reflect a particular flexibility to acclimate to varying light conditions with depth or the capacity to occupy a very specific spatial ecological niche in microbialites from different depths. Alternatively, Ca. L. mexicanus may also have the ability to modulate its gene expression as a function of the local environmental conditions during diel cycles in microbialites along the depth gradient.

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Auracyanin, a blue copper protein from the green photosynthetic bacterium Chloroflexus aurantiacus

Cited by 44 publications

References 39 publications

The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha

The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha

Origin and early evolution of photosynthesis

A Novel Microbialite-Associated Phototrophic Chloroflexi Lineage Exhibiting a Quasi-Clonal Pattern along Depth

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