Stability of the heme environment of the nitric oxide synthase from Staphylococcus aureus in the absence of pterin cofactor (Q34187137)

31 July 2017

title

Stability of the heme environment of the nitric oxide synthase from Staphylococcus aureus in the absence of pterin cofactor (English)

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31 July 2017

main subject

Staphylococcus aureus

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inferred from title

author name string

François J M Chartier

series ordinal

1

1 reference

31 July 2017

Manon Couture

series ordinal

2

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31 July 2017

language of work or name

English

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publication date

1 September 2004

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31 July 2017

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31 July 2017

volume

87

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31 July 2017

issue

3

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31 July 2017

page(s)

1939-1950

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

31 July 2017

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Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus

5 July 2018

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5 July 2018

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5 July 2018

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Tetrahydrobiopterin-deficient nitric oxide synthase has a modified heme environment and forms a cytochrome P-420 analogue

5 July 2018

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5 July 2018

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28 October 2018

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28 October 2018

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12 December 2020

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12 December 2020

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12 December 2020

The Heme Environment of Mouse Neuroglobin

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12 December 2020

Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: detection of Fe-CO stretching and Fe-C-O bending vibrations and influence of the quaternary structure change

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12 December 2020

CO binding study of mouse heme-regulated eIF-2alpha kinase: kinetics and resonance Raman spectra

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12 December 2020

Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism

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12 December 2020

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12 December 2020

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Tetrahydrobiopterin and endothelial nitric oxide synthase activity

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12 December 2020

10.1529/BIOPHYSJ.104.042119

Identifiers

DOI

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31 July 2017

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31 July 2017

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