A Redox-controlled Molecular Switch Revealed by the Crystal Structure of a Bacterial Heme PAS Sensor (Q27643191)

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24 November 2019

title

A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor (English)

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24 November 2019

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6

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24 November 2019

Toru Shimizu

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24 November 2019

author name string

Hirofumi Kurokawa

1

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24 November 2019

Dong-Sun Lee

2

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24 November 2019

Miki Watanabe

3

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24 November 2019

Ikuko Sagami

4

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24 November 2019

Bunzo Mikami

5

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24 November 2019

language of work or name

English

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publication date

23 February 2004

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Journal of Biological Chemistry

24 November 2019

published in

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24 November 2019

volume

279

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24 November 2019

issue

19

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24 November 2019

page(s)

20186-20193

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Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure.

24 November 2019

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Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli.

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Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli. Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met-95 mutants.

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Cloning, purification, crystallization and preliminary X-ray analysis of DOS heme domain, a new heme oxygen sensor in Escherichia coli.

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Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance Raman spectroscopic studies

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1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore

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Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction

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Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain

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21 January 2018

Identifiers

DOI

10.1074/JBC.M314199200

2 references

Consolidated OpenCitations Corpus – April 2017

469436

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24 November 2019

469436

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

469436