Redox role for tetrahydrobiopterin in nitric oxide synthase catalysis: low-temperature optical absorption spectral detection. (Q44037725)

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10 November 2019

title

Redox role for tetrahydrobiopterin in nitric oxide synthase catalysis: low-temperature optical absorption spectral detection (English)

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10 November 2019

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4

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Antonius Cornelis Franciscus Gorren

10 November 2019

series ordinal

1

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10 November 2019

author name string

Nicole Bec

series ordinal

2

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10 November 2019

Reinhard Lange

series ordinal

3

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10 November 2019

language of work or name

English

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publication date

1 January 2002

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10 November 2019

published in

Methods in Enzymology

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10 November 2019

volume

353

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10 November 2019

page(s)

114-121

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Nitric oxide synthases: properties and catalytic mechanism

10 November 2019

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Reaction of neuronal nitric-oxide synthase with oxygen at low temperature. Evidence for reductive activation of the oxy-ferrous complex by tetrahydrobiopterin.

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Low-Temperature Optical Absorption Spectra Suggest a Redox Role for Tetrahydrobiopterin in Both Steps of Nitric Oxide Synthase Catalysis†

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Formation of a Pterin Radical in the Reaction of the Heme Domain of Inducible Nitric Oxide Synthase with Oxygen†

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The role of tetrahydrobiopterin in the activation of oxygen by nitric-oxide synthase

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Formation of a protonated trihydrobiopterin radical cation in the first reaction cycle of neuronal and endothelial nitric oxide synthase detected by electron paramagnetic resonance spectroscopy.

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Low-temperature stabilization and spectroscopic characterization of the dioxygen complex of the ferrous neuronal nitric oxide synthase oxygenase domain

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The ferrous-dioxy complex of neuronal nitric oxide synthase. Divergent effects of L-arginine and tetrahydrobiopterin on its stability

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The Ferrous Dioxygen Complex of the Oxygenase Domain of Neuronal Nitric-oxide Synthase

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7 January 2021

Formation and reactions of the heme-dioxygen intermediate in the first and second steps of nitric oxide synthesis as studied by stopped-flow spectroscopy under single-turnover conditions

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7 January 2021

The rapid-flow-quench method in the study of fast reactions in biochemistry: extension to subzero conditions

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7 January 2021

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Identifiers

DOI

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10 November 2019

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