Observation of fast release of NO from ferrousd1haem allows formulation of a unified reaction mechanism for cytochromecd1nitrite reductases (Q58069875)

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scientific article published on 01 April 2011

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English	Observation of fast release of NO from ferrousd1haem allows formulation of a unified reaction mechanism for cytochromecd1nitrite reductases	scientific article published on 01 April 2011

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20 January 2020

Observation of fast release of NO from ferrous d₁ haem allows formulation of a unified reaction mechanism for cytochrome cd₁ nitrite reductases (English)

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20 January 2020

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20 January 2020

Alessandro Arcovito

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20 January 2020

Maurizio Brunori

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20 January 2020

Francesca Cutruzzola'

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20 January 2020

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Nicoletta Castiglione

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20 January 2020

Valentina Stelitano

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20 January 2020

Katharine A Sam

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20 January 2020

James W A Allen

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20 January 2020

Stuart J Ferguson

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20 January 2020

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1 April 2011

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20 January 2020

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9

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Biochemical Journal

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20 January 2020

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20 January 2020

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20 January 2020

217-225

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Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme

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Fast Dissociation of Nitric Oxide from FerrousPseudomonas aeruginosacd1Nitrite Reductase

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Nitrite controls the release of nitric oxide in Pseudomonas aeruginosa cd1 nitrite reductase.

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Cytochrome cd1, reductive activation and kinetic analysis of a multifunctional respiratory enzyme

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Pulse radiolysis studies on cytochrome cd1 nitrite reductase from Thiosphaera pantotropha: evidence for a fast intramolecular electron transfer from c-heme to d1-heme

1 reference

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Intramolecular electron transfer in Pseudomonas aeruginosa cd(1) nitrite reductase: thermodynamics and kinetics

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X-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus

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Redox control of fast ligand dissociation from Escherichia coli cytochrome bd.

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Unexpected dependence on pH of NO release from Paracoccus pantotrophus cytochrome cd1.

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Very early reaction intermediates detected by microsecond time scale kinetics of cytochrome cd1-catalyzed reduction of nitrite

1 reference

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Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine.

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The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties

1 reference

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Cyanide binding to cd(1) nitrite reductase from Pseudomonas aeruginosa: role of the active-site His369 in ligand stabilization

1 reference

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Allosteric control of internal electron transfer in cytochrome cd1 nitrite reductase.

1 reference

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Allosteric cooperative interactions among redox sites of Pseudomonas cytochrome oxidase

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The Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase

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Nitrite as regulator of hypoxic signaling in mammalian physiology

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The functional nitrite reductase activity of the heme-globins

1 reference

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21 January 2018

Rates of nitric oxide dissociation from hemoglobin

1 reference

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Nitrite reduction: a ubiquitous function from a pre-aerobic past.

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1 reference

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Identifiers

10.1042/BJ20101615

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21244362%20AND%20SRC:MED&resulttype=core&format=json

20 January 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21244362%20AND%20SRC:MED&resulttype=core&format=json

20 January 2020

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