The structure of cbb3 cytochrome oxidase provides insights into proton pumping (Q27662718)

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English	The structure of cbb3 cytochrome oxidase provides insights into proton pumping	scientific article

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instance of

scholarly article

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title

The structure of cbb3 cytochrome oxidase provides insights into proton pumping (English)

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author

Ulrich Ermler

series ordinal

5

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Eberhard Warkentin

series ordinal

2

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Hartmut Michel

series ordinal

6

object named as

Hartmut Michel

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author name string

Sabine Buschmann

series ordinal

1

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Hao Xie

series ordinal

3

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Julian D Langer

series ordinal

4

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language of work or name

English

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publication date

16 July 2010

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published in

Science

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volume

329

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issue

5989

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page(s)

327-30

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cites work

Energy transduction: proton transfer through the respiratory complexes

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Crossref

reference URL

https://api.crossref.org/works/10.1126/SCIENCE.1187303

retrieved

20 April 2017

Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody F V fragment

1 reference

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Crossref

reference URL

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20 April 2017

The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides

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reference URL

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20 April 2017

The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site

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reference URL

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20 April 2017

Structure and mechanism of the aberrant ba3-cytochrome c oxidase from Thermus thermophilus

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Crossref

reference URL

https://api.crossref.org/works/10.1126/SCIENCE.1187303

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20 April 2017

Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Vectorial proton transfer coupled to reduction of O2 and NO by a heme-copper oxidase

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Stability of the cbb3-type cytochrome oxidase requires specific CcoQ-CcoP interactions

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11 October 2022

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

A pathway for protons in nitric oxide reductase from Paracoccus denitrificans

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11 October 2022

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Molecular and spectroscopic analysis of the cytochrome cbb(3) oxidase from Pseudomonas stutzeri

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

The cbb3 oxidases are an ancient innovation of the domain bacteria.

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Active site of cytochrome cbb3.

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: new insights into the active site and the proton transfer pathways

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

The symbiotically essential cbb(3)-type oxidase of Bradyrhizobium japonicum is a proton pump

1 reference

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

The bacterial cytochrome cbb3 oxidases

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COCI

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11 October 2022

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Darwin at the molecular scale: selection and variance in electron tunnelling proteins including cytochrome c oxidase

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COCI

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11 October 2022

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases

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COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Two conserved non-canonical histidines are essential for activity of the cbb (3)-type oxidase in Rhodobacter capsulatus: non-canonical histidines are essential for cbb (3)-type oxidase activity in R. capsulatus

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COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Modeling the active-site structure of the cbb3-type oxidase from Rhodobacter sphaeroides

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COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Sequence analysis of the cbb3 oxidases and an atomic model for the Rhodobacter sphaeroides enzyme.

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COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A

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COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Looking for the minimum common denominator in haem-copper oxygen reductases: towards a unified catalytic mechanism

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Kinetic trapping of oxygen in cell respiration

1 reference

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COCI

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11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Identification of a histidine-tyrosine cross-link in the active site of the cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides

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COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Comparative genomics and site-directed mutagenesis support the existence of only one input channel for protons in the C-family (cbb3 oxidase) of heme-copper oxygen reductases

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stated in

COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Electron transfer and energy transduction in the terminal part of the respiratory chain - lessons from bacterial model systems

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COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Role of Campylobacter jejuni respiratory oxidases and reductases in host colonization

1 reference

stated in

COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping

1 reference

stated in

COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Properties of the detergent solubilised cytochrome c oxidase (cytochrome cbb(3)) purified from Pseudomonas stutzeri

1 reference

stated in

COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase

1 reference

stated in

COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum

1 reference

stated in

COCI

retrieved

11 October 2022

reference URL

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1187303

Identifiers

DOI

10.1126/SCIENCE.1187303

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4984115

ADS bibcode

2010Sci...329..327B

0 references

OpenCitations bibliographic resource ID

4984115

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4984115

PubMed publication ID

20576851

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4984115

ResearchGate publication ID

44798908

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