(Q36860300)

English

Purification and spectroscopic characterization of Ctb, a group III truncated hemoglobin implicated in oxygen metabolism in the food-borne pathogen Campylobacter jejuni

scientific article published on May 2006

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Purification and spectroscopic characterization of Ctb, a group III truncated hemoglobin implicated in oxygen metabolism in the food-borne pathogen Campylobacter jejuni (English)

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

1 reference

based on heuristic

inferred from title

Campylobacter jejuni

object named as

Campylobacter jejuni

1 reference

based on heuristic

inferred from title

author name string

Laura M Wainwright

1

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Yinghua Wang

2

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Simon F Park

3

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Syun-Ru Yeh

4

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Robert K Poole

5

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

language of work or name

0 references

publication date

1 May 2006

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

45

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

19

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

6003-6011

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Is bound carbonyl linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data

1 reference

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Three globin lineages belonging to two structural classes in genomes from the three kingdoms of life

1 reference

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NssR, a member of the Crp-Fnr superfamily from Campylobacter jejuni, regulates a nitrosative stress-responsive regulon that includes both a single-domain and a truncated haemoglobin

1 reference

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29 September 2017

Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy

1 reference

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29 September 2017

Role of an inducible single-domain hemoglobin in mediating resistance to nitric oxide and nitrosative stress in Campylobacter jejuni and Campylobacter coli

1 reference

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The absence of proximal strain in the truncated hemoglobins from Mycobacterium tuberculosis

1 reference

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The crystal structure of Synechocystis hemoglobin with a covalent heme linkage

1 reference

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29 September 2017

Microbial globins

1 reference

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29 September 2017

Reactions of Mycobacterium tuberculosis Truncated Hemoglobin O with Ligands Reveal a Novel Ligand-Inclusive Hydrogen Bond Network

1 reference

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29 September 2017

A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O.

1 reference

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Bacterial hemoglobins and flavohemoglobins for alleviation of nitrosative stress in Escherichia coli.

1 reference

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29 September 2017

Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases

1 reference

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29 September 2017

Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide

1 reference

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29 September 2017

Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis

1 reference

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29 September 2017

Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli

1 reference

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Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2528550

29 September 2017

Mycobacterium tuberculosis hemoglobin N displays a protein tunnel suited for O2 diffusion to the heme

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2528550

29 September 2017

Flavohemoglobin, a globin with a peroxidase-like catalytic site

1 reference

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29 September 2017

New functions for the ancient globin family: bacterial responses to nitric oxide and nitrosative stress

1 reference

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29 September 2017

A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2528550

29 September 2017

Protection from nitrosative stress by yeast flavohemoglobin

1 reference

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29 September 2017

A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis

1 reference

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29 September 2017

Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands

1 reference

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29 September 2017

Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni

1 reference

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29 September 2017

The oxygen affinity of cytochrome bo' in Escherichia coli determined by the deoxygenation of oxyleghemoglobin and oxymyoglobin: Km values for oxygen are in the submicromolar range

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2528550

29 September 2017

The iron-proximal histidine linkage and protein control of oxygen binding in hemoglobin. A transient Raman study

1 reference

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29 September 2017

High efficiency transformation of Escherichia coli with plasmids

1 reference

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29 September 2017

NO binding induced conformational changes in a truncated hemoglobin from Mycobacterium tuberculosis

1 reference

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Ligand binding in the ferric and ferrous states of Paramecium hemoglobin.

1 reference

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The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition.

1 reference

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Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide: evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing.

1 reference

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Redox equilibrium of sperm-whale myoglobin, Aplysia myoglobin, and Chironomus thummi hemoglobin

1 reference

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Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems

1 reference

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Electron-accepting properties of cytochrome o purified from Vitreoscilla.

1 reference

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Hemoglobins dioxygenate nitric oxide with high fidelity

1 reference

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4 September 2018

A truncated haemoglobin implicated in oxygen metabolism by the microaerophilic food-borne pathogen Campylobacter jejuni

1 reference

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1 reference

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The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties

1 reference

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1 reference

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4 September 2018

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1 reference

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4 September 2018

Role for the Salmonella flavohemoglobin in protection from nitric oxide

1 reference

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Membrane D-lactate oxidase in Zymomonas mobilis: evidence for a branched respiratory chain

1 reference

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12 December 2020

based on heuristic

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Theoretical Study of the Truncated Hemoglobin HbN: Exploring the Molecular Basis of the NO Detoxification Mechanism

1 reference

https://pubmed.ncbi.nlm.nih.gov/16681372

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a "Nitric oxide Releaser," and paraquat and is essential for transcriptional responses to oxidative stress

1 reference

https://pubmed.ncbi.nlm.nih.gov/16681372

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A Cooperative Oxygen Binding Hemoglobin fromMycobacterium tuberculosis

1 reference

https://pubmed.ncbi.nlm.nih.gov/16681372

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket

1 reference

https://pubmed.ncbi.nlm.nih.gov/16681372

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI052247K

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

ResearchGate publication ID

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