Heme environmental structure of CooA is modulated by the target DNA binding. Evidence from resonance Raman spectroscopy and CO rebinding kinetics (Q38335080)

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English	Heme environmental structure of CooA is modulated by the target DNA binding. Evidence from resonance Raman spectroscopy and CO rebinding kinetics	scientific article

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scholarly article

1 reference

Europe PubMed Central

2 September 2017

Heme environmental structure of CooA is modulated by the target DNA binding. Evidence from resonance Raman spectroscopy and CO rebinding kinetics (English)

1 reference

Europe PubMed Central

2 September 2017

author name string

Uchida T

1

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Europe PubMed Central

2 September 2017

Ishikawa H

2

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Europe PubMed Central

2 September 2017

Takahashi S

3

1 reference

Europe PubMed Central

2 September 2017

Ishimori K

4

1 reference

Europe PubMed Central

2 September 2017

Morishima I

5

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Europe PubMed Central

2 September 2017

Ohkubo K

6

1 reference

Europe PubMed Central

2 September 2017

Nakajima H

7

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2 September 2017

Aono S

8

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2 September 2017

language of work or name

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publication date

1 August 1998

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2 September 2017

Journal of Biological Chemistry

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2 September 2017

273

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2 September 2017

32

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Europe PubMed Central

2 September 2017

19988-19992

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Europe PubMed Central

2 September 2017

A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.32.19988

21 January 2018

CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein

1 reference

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21 January 2018

Regulation of carbon monoxide dehydrogenase and hydrogenase in Rhodospirillum rubrum: effects of CO and oxygen on synthesis and activity

1 reference

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21 January 2018

Carbon monoxide-dependent growth of Rhodospirillum rubrum

1 reference

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21 January 2018

Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system

1 reference

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21 January 2018

In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: molecular and physiological characterization of cooCTJ

1 reference

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21 January 2018

Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators

1 reference

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21 January 2018

Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme

1 reference

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21 January 2018

Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum

1 reference

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21 January 2018

Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA.

1 reference

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21 January 2018

Model of specific complex between catabolite gene activator protein and B-DNA suggested by electrostatic complementarity

1 reference

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21 January 2018

Structural determinants of the stretching frequency of CO bound to myoglobin

1 reference

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21 January 2018

The effects of heme pocket hydrophobicity on the ligand binding dynamics in myoglobin as studied with leucine 29 mutants

1 reference

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21 January 2018

Resonance Raman scattering from hemoproteins. Effects of ligands upon the Raman spectra of various C-type cytochromes

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Distal and proximal ligand interactions in heme proteins: correlations between C-O and Fe-C vibrational frequencies, oxygen-17 and carbon-13 nuclear magnetic resonance chemical shifts, and oxygen-17 nuclear quadrupole coupling constants in C17O- and

1 reference

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21 January 2018

Resonance raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement.

1 reference

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21 January 2018

The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers

1 reference

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21 January 2018

Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.32.19988

21 January 2018

Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.32.19988

21 January 2018

Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.32.19988

21 January 2018

Single Transduction in the Transcriptional Activator CooA Containing a Heme-Based CO Sensor: Isolation of a Dominant Positive Mutant Which Is Active as the Transcriptional Activator Even in the Absence of CO

1 reference

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21 January 2018

Kinetics of the reactions of Aplysia myoglobin with oxygen and carbon monoxide

1 reference

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21 January 2018

Heme-heme oxygenase complex: structure and properties of the catalytic site from resonance Raman scattering

1 reference

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21 January 2018

Structural characterization of isolated mitochondrial cytochrome c1

1 reference

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21 January 2018

Ligand-modulated binding of a gene regulatory protein to DNA. Quantitative analysis of cyclic-AMP induced binding of CRP from Escherichia coli to non-specific and specific DNA targets

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21 January 2018

Identifiers

10.1074/JBC.273.32.19988

1 reference

Europe PubMed Central

2 September 2017

1 reference

Europe PubMed Central

2 September 2017

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