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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todo:paper_00027863_v127_n21_p7721_Marti2023-10-03T13:53:45Z Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break? Martí, M.A. Capece, L. Crespo, A. Doctorovich, F. Estrin, D.A. 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 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 and transduces the NO signal. Cytochrome c′ (cyt c′) is a protobacteria heme protein that has several similarities with sGC, including the ability to form a five-coordinate NO adduct and the fact that it does not bind oxygen. Recent crystallographic characterization of cyt c′ from Alcaligenes xylosoxidans (AXCP) has yielded the discovery that exogenous ligands are able to bind to the Fe center from either side of the porphyrin plane. In this paper, we explore the molecular basis of the NO interaction with AXCP using hybrid quantum-classical simulation techniques. Our results suggest that Fe-His bond breaking depends not only on the iron-histidine bond strength but also on the existence of a local minimum conformation of the protein with the histidine away from the iron. We also show that AXCP is a useful paradigm for NO interaction with heme proteins, particularly regarding the activation/deactivation mechanism of sGC. The results presented here fully support a recently proposed model of sGC activation in which NO is not only the iron ligand but also catalyzes the activation step. © 2005 American Chemical Society. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00027863_v127_n21_p7721_Marti |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Martí, M.A. Capece, L. Crespo, A. Doctorovich, F. Estrin, D.A. Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break? |
| topic_facet |
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 |
| description |
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 and transduces the NO signal. Cytochrome c′ (cyt c′) is a protobacteria heme protein that has several similarities with sGC, including the ability to form a five-coordinate NO adduct and the fact that it does not bind oxygen. Recent crystallographic characterization of cyt c′ from Alcaligenes xylosoxidans (AXCP) has yielded the discovery that exogenous ligands are able to bind to the Fe center from either side of the porphyrin plane. In this paper, we explore the molecular basis of the NO interaction with AXCP using hybrid quantum-classical simulation techniques. Our results suggest that Fe-His bond breaking depends not only on the iron-histidine bond strength but also on the existence of a local minimum conformation of the protein with the histidine away from the iron. We also show that AXCP is a useful paradigm for NO interaction with heme proteins, particularly regarding the activation/deactivation mechanism of sGC. The results presented here fully support a recently proposed model of sGC activation in which NO is not only the iron ligand but also catalyzes the activation step. © 2005 American Chemical Society. |
| format |
JOUR |
| author |
Martí, M.A. Capece, L. Crespo, A. Doctorovich, F. Estrin, D.A. |
| author_facet |
Martí, M.A. Capece, L. Crespo, A. Doctorovich, F. Estrin, D.A. |
| author_sort |
Martí, M.A. |
| title |
Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break? |
| title_short |
Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break? |
| title_full |
Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break? |
| title_fullStr |
Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break? |
| title_full_unstemmed |
Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break? |
| title_sort |
nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. why does the iron histidine bond break? |
| url |
http://hdl.handle.net/20.500.12110/paper_00027863_v127_n21_p7721_Marti |
| work_keys_str_mv |
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| _version_ |
1807319004359950336 |