The cytochrome c domain of dimeric cytochrome cd(1...[Biochem Biophys Res Commun. 2001]

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1: Biochem Biophys Res Commun. 2001 Mar 2;281(3):788-94. Links

The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli.

Gordon EH, Steensma E, Ferguson SJ.

Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.

Cytochrome cd(1) nitrite reductase from Paracoccus pantotrophus is a dimer; within each monomer there is a largely alpha-helical domain that contains the c-type cytochrome centre. The structure of this domain changes significantly upon reduction of the heme iron, for which the ligands change from His17/His69 to Met106/His69. Overproduction, using an improved Escherichia coli expression system, of this c-type cytochrome domain as an independent monomer is reported here. The properties of the independent domain are compared with those when it is part of dimeric holo or semi-apo cytochrome cd(1). Copyright 2001 Academic Press.

PMID: 11237728 [PubMed - indexed for MEDLINE]

Heme ligation and conformational plasticity in the isolated c domain of cytochrome cd1 nitrite reductase.
J Biol Chem. 2001 Feb 23; 276(8):5846-55. Epub 2000 Oct 16.

[J Biol Chem. 2001]
Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine.
Biochemistry. 2006 Sep 19; 45(37):11208-16.

[Biochemistry. 2006]
The Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase.
J Biol Chem. 2001 Aug 3; 276(31):29450-5. Epub 2001 May 23.

[J Biol Chem. 2001]
Cytochrome cd(1) from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior.
Biochemistry. 2000 Apr 18; 39(15):4243-9.

[Biochemistry. 2000]
ReviewCytochrome cd1 nitrite reductase structure raises interesting mechanistic questions.
Subcell Biochem. 2000; 35:519-40.

[Subcell Biochem. 2000]
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Cited by 2 PubMed Central articles

A cytochrome c from a lupanine-transforming Pseudomonas putida strain is expressed in Escherichia coli during aerobic cultivation and efficiently exported and assembled in the periplasm.
Kaderbhai MA, Hopper DJ, Akhtar KM, Abbas SK, Kaderbhai NN. Appl Environ Microbiol. 2003 Aug; 69(8):4727-31.

[Appl Environ Microbiol. 2003]
Identification of two domains and distal histidine ligands to the four haems in the bacterial c-type cytochrome NapC; the prototype connector between quinol/quinone and periplasmic oxido-reductases.
Cartron ML, Roldán MD, Ferguson SJ, Berks BC, Richardson DJ. Biochem J. 2002 Dec 1; 368(Pt 2):425-32.

[Biochem J. 2002]

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The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be prod...The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli.

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The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli.

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Cited by 2 PubMed Central articles

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