Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling

Background: The HbN of Mycobacterium tuberculosis carries a potent nitric-oxide dioxygenase activity despite lacking a reductase domain. Results: The NADH-ferredoxin reductase system acts as an efficient partner for the reduction of HbN. Conclusion: The interactions of HbN with the reductase are mod...

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Detalles Bibliográficos
Autores: Singh, Sandeep, Thakur, Naveen, Oliveira, Ana, Petruk, Ariel Alcides, Hade, Mangesh Dattu, Sethi, Deepti, Bidon Chanal, Axel, Marti, Marcelo Adrian, Datta, H., Parkesh, R., Estrin, Dario Ariel, Luque, F. Javier, Dikshit, Kanak L.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/31877
Acceso en línea:http://hdl.handle.net/11336/31877
Access Level:acceso abierto
Palabra clave:Truncated hemoglobin
Tuberculosis
Electron transfer
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
Descripción
Sumario:Background: The HbN of Mycobacterium tuberculosis carries a potent nitric-oxide dioxygenase activity despite lacking a reductase domain. Results: The NADH-ferredoxin reductase system acts as an efficient partner for the reduction of HbN. Conclusion: The interactions of HbN with the reductase are modulated by its CD loop and the Pre-A region. Significance: The present study provides new insights into the mechanism of electron transfer during nitric oxide detoxification by HbN.

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