{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:01:33Z","timestamp":1791291693832,"version":"4.1.0"},"reference-count":58,"publisher":"American Chemical Society (ACS)","issue":"19","license":[{"start":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T00:00:00Z","timestamp":1790121600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T00:00:00Z","timestamp":1790121600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T00:00:00Z","timestamp":1790121600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN-2022-06130"],"award-info":[{"award-number":["RGPIN-2022-06130"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Fusobacterium nucleatum encodes HmuF, which has been shown in vitro to bind tightly to heme, traffic the cofactor to anaerobilin synthase, and catalyze the four-electron reduction of anaerobilin. The structure of the heme-bound HmuF paralog, FldH, reveals an \u03b1-helical cap appended to the flavodoxin domain. Molecular dynamics simulations of FldH without heme reveal that the \u03b1-helical cap pivots away from the flavodoxin domain to form an open complex, but then reforms the closed complex, which remains closed for the duration of the MD simulation. Transition to the open conformation disrupts noncovalent interactions formed by three conserved residues (cis-Pro151, His150, and Asp155) that form a hinge bisecting the cap and flavodoxin domain. 19F NMR was used to probe the dynamics of the cap and the role of the hinge motif. 1D NMR reveals that a single 19F-Tyr probe in the \u03b1-helical cap has two resonances that slowly exchange (\u03c4 = 1.5 ms). A H150A and D155N substitution caused coalescence of these two peaks, indicating faster exchange or stabilization of one conformer. A P151G substitution not only led to a shift in the 19F-Tyr128 peak(s), but also to the chemical shifts of the 19F-Tyr residues located in the flavodoxin fold, indicating a greater perturbation in protein structure. Despite the variants exhibiting different 19F-NMR spectra, all engage in heme trafficking and anaerobilin reduction. Together, these results indicate that while the conserved hinge fine-tunes the dynamics of the \u03b1-helical cap, this motif is not a strict prerequisite for HmuF\/FldH function.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00314","type":"journal-article","created":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T07:02:17Z","timestamp":1790146937000},"page":"3066-3079","source":"Crossref","is-referenced-by-count":0,"title":["Conserved Hinge\nMotif Modulates Conformational Mobility\nof a Heme Trafficking Protein from\n                    <i>Fusobacterium nucleatum<\/i>"],"prefix":"10.1021","volume":"65","author":[{"given":"Stella I.","family":"Widjaja","sequence":"first","affiliation":[{"name":"University of British Columbia , , Okanagan Campus, 3247 University Way , ,","place":["Kelowna, Canada, V1V 1V7"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. Hossein","family":"Khalilian","sequence":"additional","affiliation":[{"name":"University of British Columbia , , Okanagan Campus, 3247 University Way , ,","place":["Kelowna, Canada, V1V 1V7"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexandra K.","family":"McGregor","sequence":"additional","affiliation":[{"name":"University of British Columbia , , Okanagan Campus, 3247 University Way , ,","place":["Kelowna, Canada, V1V 1V7"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6132-9983","authenticated-orcid":true,"given":"Kirsten R.","family":"Wolthers","sequence":"additional","affiliation":[{"name":"University of British Columbia , , Okanagan Campus, 3247 University Way , ,","place":["Kelowna, Canada, V1V 1V7"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,23]]},"reference":[{"key":"2026100608065573400_cit1","doi-asserted-by":"publisher","first-page":"1016","DOI":"10.1038\/ismej.2012.174","article-title":"The subgingival\nmicrobiome in health and periodontitis and its relationship with community\nbiomass and inflammation","volume":"7","author":"Abusleme","year":"2013","journal-title":"ISME J."},{"key":"2026100608065573400_cit2","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1038\/s41579-018-0129-6","article-title":"Fusobacterium nucleatum\n- symbiont, opportunist and\noncobacterium","volume":"17","author":"Brennan","year":"2019","journal-title":"Nat. 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Bacteriol."},{"issue":"1","key":"2026100608065573400_cit14","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.abb.2008.10.013","article-title":"Bacterial heme-transport\nproteins and their heme-coordination modes","volume":"481","author":"Tong","year":"2009","journal-title":"Arch. Biochem. Biophys."},{"key":"2026100608065573400_cit15","doi-asserted-by":"publisher","first-page":"1781","DOI":"10.1016\/j.bbamem.2007.07.026","article-title":"Structural biology\nof bacterial iron uptake","volume":"1778","author":"Krewulak","year":"2008","journal-title":"Biochim. Biophys.\nActa, Biomembr."},{"key":"2026100608065573400_cit16","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1007\/BF02464907","article-title":"Transport across the Outer-Membrane\nof Escherichia-Coli-K12 Via the\nFhua Receptor Is Regulated by the Tonb Protein of the Cytoplasmic\nMembrane","volume":"217","author":"Scho\u0308ffler","year":"1989","journal-title":"Mol. Gen. 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Cell Biol."},{"key":"2026100608065573400_cit37","doi-asserted-by":"publisher","first-page":"4573","DOI":"10.1021\/ja00768a027","article-title":"Magnetic resonance studies of protein-small\nmolecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine\nto -chymotrypsin","volume":"94","author":"Gammon","year":"1972","journal-title":"J. Am. Chem. Soc."},{"key":"2026100608065573400_cit38","doi-asserted-by":"publisher","first-page":"469","DOI":"10.1073\/pnas.71.2.469","article-title":"Fluorotyrosine\nalkaline phosphatase\nfrom Escherichia coli: preparation,\nproperties, and fluorine-19 nuclear magnetic resonance spectrum","volume":"71","author":"Sykes","year":"1974","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026100608065573400_cit39","doi-asserted-by":"publisher","first-page":"13081","DOI":"10.1016\/S0021-9258(19)38622-3","article-title":"Activation\nof the phosphosignaling protein CheY. I. Analysis of the phosphorylated\nconformation by 19F NMR and protein engineering","volume":"268","author":"Drake","year":"1993","journal-title":"J. Biol. Chem."},{"key":"2026100608065573400_cit40","doi-asserted-by":"publisher","DOI":"10.1016\/j.abb.2025.110520","article-title":"Direct\niron-protein\ncoordination is dispensable for heme trafficking and the tetrapyrrole\nreductase activity of HmuF from Fusobacterium nucleatum","volume":"771","author":"McGregor","year":"2025","journal-title":"Arch. Biochem. Biophys."},{"key":"2026100608065573400_cit41","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1016\/j.str.2021.09.009","article-title":"Small,\nbut powerful and attractive: (19)F in biomolecular NMR","volume":"30","author":"Gronenborn","year":"2022","journal-title":"Structure"},{"key":"2026100608065573400_cit42","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bb.25.060196.001115","article-title":"Use of 19F NMR to probe protein structure\nand conformational\nchanges","volume":"25","author":"Danielson","year":"1996","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"2026100608065573400_cit43","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.pnmrs.2011.06.003","article-title":"Current applications\nof 19F NMR to studies of protein\nstructure and dynamics","volume":"62","author":"Kitevski-LeBlanc","year":"2012","journal-title":"Prog. Nucl. Magn. Reson.\nSpectrosc."},{"key":"2026100608065573400_cit44","doi-asserted-by":"publisher","DOI":"10.1002\/chem.202402820","article-title":"Fluorine Labeling and (19)F NMR Spectroscopy to Study\nBiological Molecules and Molecular Complexes","volume":"31","author":"Werle","year":"2025","journal-title":"Chem. \u2013 Eur. J."},{"key":"2026100608065573400_cit45","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2024.107122","article-title":"Structure, dynamics, and redox reactivity\nof an all-purpose flavodoxin","volume":"300","author":"Khan","year":"2024","journal-title":"J. Biol. Chem."},{"key":"2026100608065573400_cit46","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1007\/s10858-009-9359-2","article-title":"Approaches\nfor the measurement of\nsolvent exposure in proteins by 19F NMR","volume":"45","author":"Kitevski-LeBlanc","year":"2009","journal-title":"J.\nBiomol. NMR"},{"key":"2026100608065573400_cit47","doi-asserted-by":"publisher","DOI":"10.1021\/bi00240a019","article-title":"Open conformation of a substrate-binding cleft: 19F\nNMR studies of cleft angle in the D-galactose chemosensory receptor","volume":"30","author":"Luck","year":"1991","journal-title":"Biochemistry"},{"key":"2026100608065573400_cit48","first-page":"283","article-title":"Conformation\nof Polypeptides and Proteins","volume-title":"Advances\nin Protein Chemistry","author":"Ramachandran","year":"1968"},{"key":"2026100608065573400_cit49","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1111\/j.1399-3011.1973.tb02324.x","article-title":"An abinitio quantum-mechanical\ninvestigation on the\nrotational isomerism in amides and esters","volume":"5","author":"Perricaudet","year":"1973","journal-title":"Int.\nJ. Pept. Protein Res."},{"key":"2026100608065573400_cit50","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1007\/s00726-013-1511-3","article-title":"Cis-trans isomerization of omega\ndihedrals in proteins","volume":"45","author":"Craveur","year":"2013","journal-title":"Amino Acids"},{"key":"2026100608065573400_cit51","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1023\/A:1018380509735","article-title":"Backbone dynamics\nof oxidized and reduced D. vulgaris flavodoxin in solution","volume":"10","author":"Hrovat","year":"1997","journal-title":"J. Biomol. NMR"},{"key":"2026100608065573400_cit52","doi-asserted-by":"publisher","first-page":"397","DOI":"10.1016\/0022-2836(91)90721-H","article-title":"Influence of proline residues on protein conformation","volume":"218","author":"MacArthur","year":"1991","journal-title":"J. Mol. Biol."},{"key":"2026100608065573400_cit53","doi-asserted-by":"publisher","first-page":"589","DOI":"10.1002\/prot.20342","article-title":"Conservation of cis prolyl bonds in proteins during\nevolution","volume":"58","author":"Lorenzen","year":"2005","journal-title":"Proteins"},{"key":"2026100608065573400_cit54","doi-asserted-by":"publisher","first-page":"939","DOI":"10.1046\/j.1432-1327.1999.00133.x","article-title":"Site-directed\nmutagenesis of proline 204 in the \u2019hinge\u2019 region of\nyeast phosphoglycerate kinase","volume":"259","author":"McHarg","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"2026100608065573400_cit55","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1110\/ps.8.1.96","article-title":"On the role\nof the cis-proline residue in the active site of DsbA","volume":"8","author":"Charbonnier","year":"1999","journal-title":"Protein Sci."},{"key":"2026100608065573400_cit56","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1016\/j.bbrc.2022.11.089","article-title":"A dimer-monomer transition captured\nby the crystal structures of cyanobacterial apo flavodoxin","volume":"639","author":"Liu","year":"2023","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2026100608065573400_cit57","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1038\/nsb0496-329","article-title":"Closure of a tyrosine\/tryptophan\naromatic gate leads to a compact fold in apo flavodoxin","volume":"3","author":"Genzor","year":"1996","journal-title":"Nat. Struct. Biol."},{"key":"2026100608065573400_cit58","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1002\/prot.21410","article-title":"Common conformational changes in\nflavodoxins induced by FMN and anion binding: the structure of Helicobacter\npylori apoflavodoxin","volume":"69","author":"Marti\u0301nez-Ju\u0301lvez","year":"2007","journal-title":"Proteins"}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.6c00314","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/65\/19\/3066\/68612514\/acs.biochem.6c00314.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/65\/19\/3066\/68612514\/acs.biochem.6c00314.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T12:49:17Z","timestamp":1791290957000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bichaw\/article\/65\/19\/3066\/5436100\/Conserved-Hinge-Motif-Modulates-Conformational"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,23]]},"references-count":58,"journal-issue":{"issue":"19","published-online":{"date-parts":[[2026,9,23]]},"published-print":{"date-parts":[[2026,10,6]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.biochem.6c00314","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,23]]}}}