Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break?

Soluble guanylate cyclase (sGC), the mammalian receptor for nitric oxide (NO), is a heme protein with a histidine as the proximal ligand. Formation of a five-coordinate heme-NO complex with the associated Fe-His bond cleavage is believed to trigger a conformational change that activates the enzyme a...

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Detalles Bibliográficos
Autores principales: Martí, M.A., Capece, L., Crespo, A., Doctorovich, F., Estrin, D.A.
Formato: JOUR
Materias:
Activation analysis
Catalysis
Chemical bonds
Complexation
Conformations
Crystallography
Enzymes
Conformational changes
Deactivation
Ligands
Soluble guanylate cyclase (sGC)
Nitrogen oxides
cytochrome c
guanylate cyclase
hemoprotein
histidine
iron
ligand
nitric oxide
Achromobacter xylosoxidans
article
catalysis
complex formation
energy
enzyme activation
nonhuman
oxygen affinity
structure analysis
X ray crystallography
Alcaligenes
Cytochromes c'
Guanylate Cyclase
Histidine
Models, Molecular
Nitric Oxide
Protein Conformation
Thermodynamics
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00027863_v127_n21_p7721_Marti
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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