The alternative complex III A different architecture using known building modules

Manuela Alexandra Pereira; Miguel Nuno Teixeira

doi:10.1016/j.bbabio.2010.04.012

The alternative complex III A different architecture using known building modules

Manuela Alexandra Pereira, Miguel Nuno Teixeira

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

Research output: Contribution to journal › Article › peer-review

36 Citations (Scopus)

Abstract

Until recently cytochrome bc(1) complexes were the only enzymes known to be able to transfer electrons from reduced quinones to cytochrome c However a complex with the same activity and with a unique subunit composition was purified from the membranes of Rhodothermu marinus This complex named alternative complex III (ACIII) was then biochemical spectroscopic and genatically characterized Later it was observed that the presence of ACIII was not exclusive of R marinus being the genes coding for ACIII widespread at least in the Bacteria domain In this work a comprehensive description of the current knowledge on ACIII is presented The relation of ACIII with members of the complex Iron-sulfur molybdoenzyme family is investigated by analyzing all the available completely sequenced genomes It is concluded that ACIII is a new complex composed by a novel combination of modules already identified in other respiratory complexes

Original language	Unknown
Pages (from-to)	1869-1876
Journal	Biochimica Et Biophysica Acta-Bioenergetics
Volume	1797
Issue number	12
DOIs	https://doi.org/10.1016/j.bbabio.2010.04.012
Publication status	Published - 1 Jan 2010

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10.1016/j.bbabio.2010.04.012

Cite this

@article{694a2e8b634d4656b5bf22d5b09ea0d3,

title = "The alternative complex III A different architecture using known building modules",

abstract = "Until recently cytochrome bc(1) complexes were the only enzymes known to be able to transfer electrons from reduced quinones to cytochrome c However a complex with the same activity and with a unique subunit composition was purified from the membranes of Rhodothermu marinus This complex named alternative complex III (ACIII) was then biochemical spectroscopic and genatically characterized Later it was observed that the presence of ACIII was not exclusive of R marinus being the genes coding for ACIII widespread at least in the Bacteria domain In this work a comprehensive description of the current knowledge on ACIII is presented The relation of ACIII with members of the complex Iron-sulfur molybdoenzyme family is investigated by analyzing all the available completely sequenced genomes It is concluded that ACIII is a new complex composed by a novel combination of modules already identified in other respiratory complexes",

keywords = "C NITRITE REDUCTASE, RESPIRATORY-CHAIN, ELECTRON-TRANSFER CHAIN, IRON-SULFUR CENTERS, ESCHERICHIA-COLI, CYTOCHROME-C, WOLINELLA-SUCCINOGENES, ANGSTROM RESOLUTION, COPPER OXYGEN REDUCTASES, BACTERIUM RHODOTHERMUS-MARINUS",

author = "Pereira, {Manuela Alexandra} and Teixeira, {Miguel Nuno}",

note = "Refojo, Patricia N. Sousa, Filipa L.",

year = "2010",

month = jan,

day = "1",

doi = "10.1016/j.bbabio.2010.04.012",

language = "Unknown",

volume = "1797",

pages = "1869--1876",

journal = "Biochimica Et Biophysica Acta-Bioenergetics",

issn = "0005-2728",

publisher = "Elsevier Science B.V., Inc",

number = "12",

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TY - JOUR

T1 - The alternative complex III A different architecture using known building modules

AU - Pereira, Manuela Alexandra

AU - Teixeira, Miguel Nuno

N1 - Refojo, Patricia N. Sousa, Filipa L.

PY - 2010/1/1

Y1 - 2010/1/1

N2 - Until recently cytochrome bc(1) complexes were the only enzymes known to be able to transfer electrons from reduced quinones to cytochrome c However a complex with the same activity and with a unique subunit composition was purified from the membranes of Rhodothermu marinus This complex named alternative complex III (ACIII) was then biochemical spectroscopic and genatically characterized Later it was observed that the presence of ACIII was not exclusive of R marinus being the genes coding for ACIII widespread at least in the Bacteria domain In this work a comprehensive description of the current knowledge on ACIII is presented The relation of ACIII with members of the complex Iron-sulfur molybdoenzyme family is investigated by analyzing all the available completely sequenced genomes It is concluded that ACIII is a new complex composed by a novel combination of modules already identified in other respiratory complexes

AB - Until recently cytochrome bc(1) complexes were the only enzymes known to be able to transfer electrons from reduced quinones to cytochrome c However a complex with the same activity and with a unique subunit composition was purified from the membranes of Rhodothermu marinus This complex named alternative complex III (ACIII) was then biochemical spectroscopic and genatically characterized Later it was observed that the presence of ACIII was not exclusive of R marinus being the genes coding for ACIII widespread at least in the Bacteria domain In this work a comprehensive description of the current knowledge on ACIII is presented The relation of ACIII with members of the complex Iron-sulfur molybdoenzyme family is investigated by analyzing all the available completely sequenced genomes It is concluded that ACIII is a new complex composed by a novel combination of modules already identified in other respiratory complexes

KW - C NITRITE REDUCTASE

KW - RESPIRATORY-CHAIN

KW - ELECTRON-TRANSFER CHAIN

KW - IRON-SULFUR CENTERS

KW - ESCHERICHIA-COLI

KW - CYTOCHROME-C

KW - WOLINELLA-SUCCINOGENES

KW - ANGSTROM RESOLUTION

KW - COPPER OXYGEN REDUCTASES

KW - BACTERIUM RHODOTHERMUS-MARINUS

U2 - 10.1016/j.bbabio.2010.04.012

DO - 10.1016/j.bbabio.2010.04.012

M3 - Article

VL - 1797

SP - 1869

EP - 1876

JO - Biochimica Et Biophysica Acta-Bioenergetics

JF - Biochimica Et Biophysica Acta-Bioenergetics

SN - 0005-2728

IS - 12

ER -