(Q38344874)

English

One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase

scientific article published on June 1997

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scholarly article

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Europe PubMed Central

PubMed publication ID

2 September 2017

One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase (English)

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Europe PubMed Central

PubMed publication ID

2 September 2017

Escherichia coli

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author name string

J N Rumbley

1

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

E Furlong Nickels

2

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

R B Gennis

3

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Europe PubMed Central

PubMed publication ID

2 September 2017

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publication date

1 June 1997

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PubMed publication ID

2 September 2017

number of pages

12

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Biochimica et Biophysica Acta

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Europe PubMed Central

PubMed publication ID

2 September 2017

1340

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Europe PubMed Central

PubMed publication ID

2 September 2017

1

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Europe PubMed Central

PubMed publication ID

2 September 2017

131-142

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Europe PubMed Central

PubMed publication ID

2 September 2017

The superfamily of heme-copper respiratory oxidases

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Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo.

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Binuclear centre structure of terminal protonmotive oxidases

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Identification of a "peroxy" intermediate in cytochrome bo3 of Escherichia coli

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Distinct forms of the haem o-Cu binuclear site of oxidised cytochrome bo from Escherichia coli. Evidence from optical and EPR spectroscopy.

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Demonstration by FTIR that the bo-type ubiquinol oxidase of Escherichia coli contains a heme-copper binuclear center similar to that in cytochrome c oxidase and that proper assembly of the binuclear center requires the cyoE gene product.

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Oxygen reaction and proton uptake in helix VIII mutants of cytochrome bo3.

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

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Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å

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

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Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity.

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Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: EPR and Fourier transform infrared spectroscopic studies.

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Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus

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The high-level expression in Escherichia coli of the membrane-bound form of human and rat cytochrome b5 and studies on their mechanism of function

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Rapid purification of wildtype and mutant cytochrome c oxidase from Rhodobacter sphaeroides by Ni(2+)-NTA affinity chromatography

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The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type.

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Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension

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Studies on the electron transport system. XX. Chemical and physical properties of the coenzyme Q family of compounds

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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The heme groups of cytochrome o from Escherichia coli

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Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase

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On the role of quinones in bacterial electron transport. The respiratory system of Bacillus megaterium

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The kinetics of the redox reactions of ubiquinone related to the electron-transport activity in the respiratory chain.

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Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule.

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Intramolecular electron transfer in cytochrome o of Escherichia coli: events following the photolysis of fully and partially reduced CO-bound forms of the bo3 and oo3 enzymes.

1 reference

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Magnetic-circular-dichroism studies of Escherichia coli cytochrome bo. Identification of high-spin ferric, low-spin ferric and ferryl [Fe(IV)] forms of heme o.

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Interconversion of fast and slow forms of cytochrome bo from Escherichia coli.

1 reference

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Stabilization of a semiquinone radical at the high‐affinity quinone‐binding site (QH) of the Escherichia coli bo‐type ubiquinol oxidase

1 reference

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Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo

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Identifiers

10.1016/S0167-4838(97)00036-8

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

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