Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane
Abstract The interactions of nitric oxide (NO) and organic nitroso compounds with heme proteins are biologically important, and adduct formation between NO‐containing compounds and myoglobin (Mb) have served as prototypical systems for studies of these interactions. We have prepared crystals of hors...
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crwiley:10.1002/prot.10495 2024-06-23T07:56:59+00:00 Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane Copeland, Daniel M. West, Ann H. Richter‐Addo, George B. 2003 http://dx.doi.org/10.1002/prot.10495 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.10495 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.10495 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Proteins: Structure, Function, and Bioinformatics volume 53, issue 2, page 182-192 ISSN 0887-3585 1097-0134 journal-article 2003 crwiley https://doi.org/10.1002/prot.10495 2024-06-06T04:23:54Z Abstract The interactions of nitric oxide (NO) and organic nitroso compounds with heme proteins are biologically important, and adduct formation between NO‐containing compounds and myoglobin (Mb) have served as prototypical systems for studies of these interactions. We have prepared crystals of horse heart (hh) MbNO from nitrosylation of aqua‐met Mb crystals, and we have determined the crystal structure of hh MbNO at a resolution of 1.9 Å. The Fe‐N‐O angle of 147° in hh MbNO is larger than the corresponding 112° angle previously determined from the crystal structure of sperm whale MbNO (Brucker et al., Proteins 1998;30:352–356) but is similar to the 150° angle determined from a MS XAFS study of a frozen solution of hh MbNO (Rich et al., J Am Chem Soc 1998;120:10827–10836). The Fe‐N(O) bond length of 2.0 Å (this work) is longer than the 1.75 Å distance determined from the XAFS study and suggests distal pocket influences on FeNO geometry. The nitrosyl N atom is located 3.0 Å from the imidazole N ϵ atom of the distal His64 residue, suggesting electrostatic stabilization of the FeNO moiety by His64. The crystal structure of the nitrosoethane adduct of ferrous hh Mb was determined at a resolution of 1.7 Å. The nitroso O atom of the EtNO ligand is located 2.7 Å from the imidazole N ϵ atom of His64, suggesting a hydrogen bond interaction between these groups. To the best of our knowledge, the crystal structure of hh Mb(EtNO) is the first such determination of a nitrosoalkane adduct of a heme protein. Proteins 2003. © 2003 Wiley‐Liss, Inc. Article in Journal/Newspaper Sperm whale Wiley Online Library Proteins: Structure, Function, and Bioinformatics 53 2 182 192 |
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Abstract The interactions of nitric oxide (NO) and organic nitroso compounds with heme proteins are biologically important, and adduct formation between NO‐containing compounds and myoglobin (Mb) have served as prototypical systems for studies of these interactions. We have prepared crystals of horse heart (hh) MbNO from nitrosylation of aqua‐met Mb crystals, and we have determined the crystal structure of hh MbNO at a resolution of 1.9 Å. The Fe‐N‐O angle of 147° in hh MbNO is larger than the corresponding 112° angle previously determined from the crystal structure of sperm whale MbNO (Brucker et al., Proteins 1998;30:352–356) but is similar to the 150° angle determined from a MS XAFS study of a frozen solution of hh MbNO (Rich et al., J Am Chem Soc 1998;120:10827–10836). The Fe‐N(O) bond length of 2.0 Å (this work) is longer than the 1.75 Å distance determined from the XAFS study and suggests distal pocket influences on FeNO geometry. The nitrosyl N atom is located 3.0 Å from the imidazole N ϵ atom of the distal His64 residue, suggesting electrostatic stabilization of the FeNO moiety by His64. The crystal structure of the nitrosoethane adduct of ferrous hh Mb was determined at a resolution of 1.7 Å. The nitroso O atom of the EtNO ligand is located 2.7 Å from the imidazole N ϵ atom of His64, suggesting a hydrogen bond interaction between these groups. To the best of our knowledge, the crystal structure of hh Mb(EtNO) is the first such determination of a nitrosoalkane adduct of a heme protein. Proteins 2003. © 2003 Wiley‐Liss, Inc. |
format |
Article in Journal/Newspaper |
author |
Copeland, Daniel M. West, Ann H. Richter‐Addo, George B. |
spellingShingle |
Copeland, Daniel M. West, Ann H. Richter‐Addo, George B. Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane |
author_facet |
Copeland, Daniel M. West, Ann H. Richter‐Addo, George B. |
author_sort |
Copeland, Daniel M. |
title |
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane |
title_short |
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane |
title_full |
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane |
title_fullStr |
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane |
title_full_unstemmed |
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane |
title_sort |
crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane |
publisher |
Wiley |
publishDate |
2003 |
url |
http://dx.doi.org/10.1002/prot.10495 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.10495 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.10495 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Proteins: Structure, Function, and Bioinformatics volume 53, issue 2, page 182-192 ISSN 0887-3585 1097-0134 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/prot.10495 |
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Proteins: Structure, Function, and Bioinformatics |
container_volume |
53 |
container_issue |
2 |
container_start_page |
182 |
op_container_end_page |
192 |
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1802650400757645312 |