{"doi":"10.1016/j.bpj.2009.05.059","title":"The Structure of Neuroglobin at High Xe and Kr Pressure Reveals Partial Conservation of Globin Internal Cavities","abstract":null,"journal":"Biophysical Journal","year":2009,"id":656028,"datarank":0.5375278407684165,"base_score":3.58351893845611,"endowment":3.58351893845611,"self_citation_contribution":0.5375278407684165,"citation_network_contribution":0.0,"self_endowment_contribution":0.5375278407684165,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":35,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1712458,"name":"Uwe Mueller","orcid":null,"position":1,"is_corresponding":false},{"id":1712459,"name":"Jörg Schulze","orcid":null,"position":2,"is_corresponding":false},{"id":1712460,"name":"Maurizio Brunori","orcid":null,"position":3,"is_corresponding":false},{"id":1712461,"name":"Beatrice Vallone","orcid":null,"position":4,"is_corresponding":false},{"id":1712457,"name":"Tommaso Moschetti","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"The Structure of Neuroglobin at High Xe and Kr Pressure Reveals Partial Conservation of Globin Internal Cavities","abstract":"Neuroglobin (Ngb) is a hexacoordinate globin expressed in the brain of vertebrates. Ferrous Ngb binds dioxygen with high affinity and the O(2) adduct is able to scavenge NO. Convincing in vitro and in vivo data indicate that Ngb is involved in neuroprotection during hypoxia and ischemia. The 3D structure of Ngb reveals the presence of a wide internal cavity connecting its heme active site with the bulk. To explore the role of this \"tunnel\" in the control of ligand binding, we determined the structure of metNgb and NgbCO equilibrated with Xe or Kr. We show four docking sites for Xe (only two for Kr); two of the four Xe sites are within the large cavity. They are only partially conserved in globins, since the two proximal Xe sites identified in myoglobin (Xe1 and Xe2) are absent in Ngb, as well as in cytoglobin. The Xe docking sites in Ngb map a pathway within the protein matrix, leading to the heme, which becomes more accessible in the ligand-bound species. This may be of significance in connection with the redox chemistry that may be the primary function of this hexacoordinate globin.","is_dataset_classified":null,"base_score":3.58351893845611,"endowment":3.58351893845611,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"19751675","pmcid":"PMC2741589","openalex_id":"https://openalex.org/W2035799882","authors":[],"funders":[{"funder_name":"Ministero dell’Istruzione, dell’Università e della Ricerca","grant_id":"RBLA03B3KC_004","title":null},{"funder_name":"Ministero dell'Istruzione dell'Università e della Ricerca","grant_id":"unidentified","title":"unidentified"}],"total_grants":2,"fwci":1.3977,"citation_percentile":0.7855668,"influential_citations":0,"citation_trend":[{"year":2012,"count":3},{"year":2013,"count":2},{"year":2014,"count":6},{"year":2015,"count":1},{"year":2016,"count":3},{"year":2017,"count":2},{"year":2018,"count":1},{"year":2019,"count":3},{"year":2020,"count":1},{"year":2021,"count":2},{"year":2022,"count":1},{"year":2023,"count":2}],"oa_status":"bronze","license":"Elsevier Non-Commercial","oa_locations":[{"url":"http://www.cell.com/article/S0006349509011606/pdf","host_type":"journal"},{"url":"http://www.cell.com/article/S0006349509011606/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0006349509011606?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0006349509011606?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.bpj.2009.05.059","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/19751675","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2741589","host_type":"repository"},{"url":"https://www.helmholtz-berlin.de/pubbin/oai_publication?VT=1&ID=-5314","host_type":"repository"},{"url":"http://hdl.handle.net/11573/229122","host_type":"repository"},{"url":"http://dx.doi.org/10.1016/j.bpj.2009.05.059","host_type":""},{"url":"https://dx.doi.org/10.1016/j.bpj.2009.05.059","host_type":""},{"url":"http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000270380800021&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a","host_type":""},{"url":"https://hdl.handle.net/11573/229122","host_type":""}],"fields_of_study":["Hemoglobin structure and function","Quantum, superfluid, helium dynamics","Neonatal Health and Biochemistry","0301 basic medicine","0303 health sciences","03 medical and health sciences","Amino Acid Sequence","Conserved Sequence","Crystallography, X-Ray","Cytoglobin","Globins","Heme","Humans","Hydrophobic and Hydrophilic Interactions","Krypton","Ligands","Models, Molecular","Molecular Sequence Data","Myoglobin","Nerve Tissue Proteins","Neuroglobin","Pressure","Protein Conformation","Sequence Alignment","Xenon"],"mesh_terms":["Neuroglobin","Cytoglobin","Amino Acid Sequence","Globins","Heme","Humans","Krypton","Ligands","Models, Molecular","Molecular Sequence Data","Myoglobin","Nerve Tissue Proteins","Pressure","Protein Conformation","Xenon","Sequence Alignment","Conserved Sequence","Crystallography, X-Ray","Hydrophobic and Hydrophilic Interactions"],"keywords":["Neuroglobin","Globin","Chemistry","High pressure","Physics","Thermodynamics","Biochemistry","Hemoglobin","Models, Molecular","Xenon","Myoglobin","Protein Conformation","Cytoglobin","Molecular Sequence Data","Biophysics","Krypton","Nerve Tissue Proteins","Heme","Crystallography, X-Ray","Ligands","Globins","Pressure","Humans","Amino Acid Sequence","cavity; krypton; neuroglobin; protein crystallography; xenon","Hydrophobic and Hydrophilic Interactions","Sequence Alignment","Conserved Sequence"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-11T19:39:41.551880Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}