Early Evolution of Cytochrome bc Complexes

Schutz, M.M.; Brugna, Myriam; Lebrun, Évelyne; Baymann, Frauke; Huber, R.; Stetter, Karl-Otto; Hauska, Günter; Toci, René; Lemesle-Meunier, Danielle; Tron, Pascale; Schmidt, Christian; Nitschke, Wolfgang

doi:10.1006/jmbi.2000.3915

Cited by 162 publications

(130 citation statements)

References 47 publications

Supporting

Mentioning

123

Contrasting

Order By: Relevance

“…Other delta-proteobacteria confidently cluster with the "B" group of ubiquinol cytochrome c reductase sequences. Notably, "B" sequences from the aquificae cluster with the epsilon-proteobacteria, suggestive of horizontal gene transfer, as reported previously (Schutz et al, 2000). Apart from the cluster of "B" sequences from the proteobacteria and the aquificae, there is a cluster of divergent "B" sequences from a mix of lineages (Opitutus terrae -verrucomicrobia, Acidobacterium capsulatum and Candidatus Solibacter usitatus -acidobacteria, Gemmatimonas aurantiacagemmatimonadetes, Candidatus Nitrospira defluvii -nitrospirae) which group with the divergent Gliobacter cytochrome b 6 "A" sequence.…”

Section: Cytochrome-b Of the B 6 F And The Bc Complexsupporting

confidence: 80%

“…Molecular evolution analysis of cytochrome-b and the ISP in 30 species (including chloroplasts, mitochondria, proteobacteria, cyanobacteria, firmicutes, chlorobi, Deinocccus, and some archaea) showed global agreement with the 16S rRNA phylogeny, with the exception of one HGT event into aquificae (Schutz et al, 2000). A subsequent analysis by the same group including more species, showed similar results, but also indicated that evolutionary reconstruction of the Rieske protein had to be guided by structure-based alignments to avoid pitfalls suggestive of multiple HGT events (Lebrun et al, 2006).…”

Section: Schutz Et Al Reviewed the Evolution Of Cytochrome Bc Complexmentioning

confidence: 71%

“…showing that the core of the complex was likely the cytochrome-b and the Rieske Iron Sulfur Protein (ISP), while the cytochrome c subunit is highly divergent and does not have a monophyletic origin (Schutz et al, 2000). Molecular evolution analysis of cytochrome-b and the ISP in 30 species (including chloroplasts, mitochondria, proteobacteria, cyanobacteria, firmicutes, chlorobi, Deinocccus, and some archaea) showed global agreement with the 16S rRNA phylogeny, with the exception of one HGT event into aquificae (Schutz et al, 2000).…”

Section: Schutz Et Al Reviewed the Evolution Of Cytochrome Bc Complexmentioning

confidence: 99%

“…Previous analyses (Schutz et al, 2000, Lebrun et al, 2006, Nitschke et al, 2010, Dibrova et al, 2013 have attempted to derive a complete phylogeny of cytochrome-b from a diverse set of prokaryotes, but they mostly focus on the comparison of cytochrome b 6 of the b 6 f complex of photosynthesis and the cytochrome bc complex of respiration. Also, in those analyses only some cytochromeb domain containing proteins were included while some other were excluded; this might skew the results, and thus the conclusions.…”

Section: Schutz Et Al Reviewed the Evolution Of Cytochrome Bc Complexmentioning

confidence: 99%

“…The b 6 f complex of photosynthetic ETCs, and the bc complex of respiratory ETCs have long been known to be homologous (Schutz et al, 2000). (Nitschke et al, 2010), based on which a grouping of the cyanobacteria, heliobacteria and chlorobi was suggested.…”

Section: Cytochrome-b Of the B 6 F And The Bc Complexmentioning

confidence: 99%

See 4 more Smart Citations

Evolution of b-type cytochromes in prokaryotes

Koumandou

Κοσσίδα

2015

Preprint

View full text Add to dashboard Cite

Abstract:Prokaryotes use a wide variety of bioenergetic pathways but the order of emergence of these pathways and their evolutionary relationships are still unresolved issues. In this study we focus on the evolutionary relationships of different families of b-type cytochromes, which form part of a variety of bioenergetic enzymes (the cytochrome b 6 f complex, ubiquinol and menaquinol reductases, formate dehydrogenase, Ni/Fehydrogenase, and succinate dehydrogenase). We use data from 272 species of fully sequenced bacteria and archaea, which represent the full diversity of prokaryotic lineages and multiple bioenergetic modes, to examine the distribution of these cytochromes across lineages, and ask the question of whether sequences from different species cluster by cytochrome-b family, by bioenergetic mode or by taxonomic group. Different cytochrome-b types are found in many lineages of the bacteria and archaea, and form distinct groups in phylogenetic analysis, which indicates an ancient origin for this complex, and diversification of different cytochrome-b types before the diversification of lineages. We find that species do not cluster based on bioenergetic mode. We also re-examine data from previous studies using this expanded sample of organisms spanning the full diversity of prokaryotic lineages. Concerning the b 6 f complex of photosynthetic organisms, our expanded phylogenies do not show significant bootstrap support for a "green clade" of cytochrome b 6 ; also, the split form of b 6 is not monophyletic, indicating that the split form arose independently multiple times. We also present data on the similarities between prokaryotic and eukaryotic cytochrome b561 sequences, in light of the recently reported structure of eukaryotic cytochrome b561.PeerJ PrePrints | https://doi.org/10.7287/peerj.preprints.1564v1 | CC-BY 4.0 Open Access |

show abstract

Section: Cytochrome-b Of the B 6 F And The Bc Complexsupporting

confidence: 80%

Section: Schutz Et Al Reviewed the Evolution Of Cytochrome Bc Complexmentioning

confidence: 71%

Section: Schutz Et Al Reviewed the Evolution Of Cytochrome Bc Complexmentioning

confidence: 99%

Section: Schutz Et Al Reviewed the Evolution Of Cytochrome Bc Complexmentioning

confidence: 99%

Section: Cytochrome-b Of the B 6 F And The Bc Complexmentioning

confidence: 99%

See 3 more Smart Citations

Evolution of b-type cytochromes in prokaryotes

Koumandou

Κοσσίδα

2015

Preprint

View full text Add to dashboard Cite

show abstract

The Cytochromeb₆Complex of Oxygenic Photosynthesis

Yamashita

Baniulis

Hasan

2004

Handbook of Metalloproteins

View full text Add to dashboard Cite

The cytochrome b 6 f complex is the central complex in the electron transport chain of oxygenic photosynthesis. It provides the electronic connection between the two photosynthetic reaction centers and generates most of the transmembrane electrochemical proton gradient that is used for ATP synthesis. It is a hetero‐oligomeric 220‐kDa homo‐dimeric complex consisting of 8 polypeptide subunits, 13 transmembrane helical segments, and 7 tightly bound prosthetic groups per monomer. It is one of relatively few hetero‐oligomeric membrane proteins whose crystal structure has been solved to a resolution ≤3.0 Å. Among the seven prosthetic groups per monomer, five have a redox function: two b ‐type hemes, b p and b n , on the electrochemically positive and negative sides of the complex, the p‐side heme of cytochrome f , a unique c ‐type cytochrome, and a p‐side [2Fe–2S] center, and a unique heme c n covalently bound to the cytochrome b subunit, which interacts electronically with hem b n . These groups are arranged to accomplish the oxidation and reduction of plastoquinol/plastoquinone (PQH 2 /PQ) on the p‐ and n‐sides of the membrane, and thereby accomplish a net transfer of as many as two protons across the membrane per electron transferred through the complex, thus providing the major input to the transmembrane proton electrochemical gradient. The redox reactions of PQ/PQH 2 occur within the two quinone‐exchange cavities formed by the two monomers of the complex. The p‐side redox reactions are similar to those of the cytochrome bc 1 complex. However, redox reactions on the n‐side are different, partly because of the presence of heme c n .

show abstract