{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T07:54:29Z","timestamp":1777535669885,"version":"3.51.4"},"reference-count":34,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2009,5,1]],"date-time":"2009-05-01T00:00:00Z","timestamp":1241136000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2009,5]]},"DOI":"10.1016\/j.bbrc.2009.03.148","type":"journal-article","created":{"date-parts":[[2009,4,3]],"date-time":"2009-04-03T08:31:12Z","timestamp":1238747472000},"page":"178-182","source":"Crossref","is-referenced-by-count":40,"title":["Heme environment in HmuY, the heme-binding protein of Porphyromonas gingivalis"],"prefix":"10.1016","volume":"383","author":[{"given":"Halina","family":"W\u00f3jtowicz","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jacek","family":"Wojaczy\u0144ski","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mariusz","family":"Olczak","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jaros\u0142aw","family":"Kr\u00f3liczewski","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lechos\u0142aw","family":"Latos-Gra\u017cy\u0144ski","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Teresa","family":"Olczak","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2009.03.148_bib1","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.femsre.2004.09.001","article-title":"Iron and heme utilization in Porphyromonas gingivalis","volume":"29","author":"Olczak","year":"2005","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.bbrc.2009.03.148_bib2","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1042\/bj3620239","article-title":"Interactions of Porphyromonas gingivalis with oxyhaemoglobin and deoxyhaemoglobin","volume":"362","author":"Smalley","year":"2002","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbrc.2009.03.148_bib3","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1042\/bj3310681","article-title":"The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the mu-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism","volume":"331","author":"Smalley","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbrc.2009.03.148_bib4","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1046\/j.1365-2958.1999.01499.x","article-title":"Interactions of HasA, a bacterial haemophore, with haemoglobin and with its outer membrane receptor HasR","volume":"33","author":"Letoffe","year":"1999","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.bbrc.2009.03.148_bib5","doi-asserted-by":"crossref","first-page":"5737","DOI":"10.1128\/JB.182.20.5737-5748.2000","article-title":"Characterization and expression of HmuR, a TonB-dependent hemoglobin receptor of Porphyromonas gingivalis","volume":"182","author":"Simpson","year":"2000","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbrc.2009.03.148_bib6","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1007\/s00203-007-0309-7","article-title":"Porphyromonas gingivalis HmuY and HmuR\u2014further characterization of a novel mechanism of heme utilization","volume":"183","author":"Olczak","year":"2008","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.bbrc.2009.03.148_bib7","doi-asserted-by":"crossref","first-page":"3367","DOI":"10.1099\/mic.0.29011-0","article-title":"Transcriptional organization, regulation and role of the Porphyromonas gingivalis W83 hmu haemin-uptake locus","volume":"152","author":"Lewis","year":"2006","journal-title":"Microbiology"},{"key":"10.1016\/j.bbrc.2009.03.148_bib8","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1006\/mpat.1996.0043","article-title":"Isolation and characterization of a hemin-binding cell envelope protein from Porphyromonas gingivalis","volume":"21","author":"Kim","year":"1996","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.bbrc.2009.03.148_bib9","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1128\/IAI.61.2.588-595.1993","article-title":"Purification and characterization of fibroblast-activating factor isolated from Porphyromonas gingivalis W50","volume":"61","author":"Mihara","year":"1993","journal-title":"Infect. Immun."},{"key":"10.1016\/j.bbrc.2009.03.148_bib10","doi-asserted-by":"crossref","first-page":"1044","DOI":"10.1128\/JB.01270-08","article-title":"Response of Porphyromonas gingivalis to heme limitation in continuous culture","volume":"191","author":"Dashper","year":"2009","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbrc.2009.03.148_bib11","doi-asserted-by":"crossref","first-page":"1645","DOI":"10.1002\/pmic.200700557","article-title":"Application of 16O\/18O reverse proteolytic labeling to determine the effect of biofilm culture on the cell envelope proteome of Porphyromonas gingivalis W50","volume":"8","author":"Ang","year":"2008","journal-title":"Proteomics"},{"key":"10.1016\/j.bbrc.2009.03.148_bib12","doi-asserted-by":"crossref","first-page":"13179","DOI":"10.1021\/bi050422r","article-title":"Characterization of the periplasmic heme-binding protein ShuT from the heme uptake system of Shigella dysenteriae","volume":"44","author":"Eakanunkul","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2009.03.148_bib13","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1006\/abio.1996.0171","article-title":"Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies","volume":"236","author":"Zor","year":"1996","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib14","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0003-2697(87)90643-9","article-title":"Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra","volume":"161","author":"Berry","year":"1987","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib15","doi-asserted-by":"crossref","first-page":"7570","DOI":"10.1021\/bi047422w","article-title":"Integration of the thylakoid membrane protein cytochrome b6 in the cytoplasmic membrane of Escherichia coli","volume":"44","author":"Kroliczewski","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2009.03.148_bib16","doi-asserted-by":"crossref","first-page":"29342","DOI":"10.1074\/jbc.270.49.29342","article-title":"Purification and characterization of the cytochrome b6f complex from Chlamydomonas reinhardtii","volume":"270","author":"Pierre","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib17","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1016\/j.jinorgbio.2007.11.011","article-title":"Heme binding in the NEAT domains of IsdA and IsdC of Staphylococcus aureus","volume":"102","author":"Pluym","year":"2008","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib18","first-page":"351","article-title":"The relevance of J cross-peaks in two-dimensional NOE experiments of macromolecules","volume":"47","author":"Macura","year":"1982","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.bbrc.2009.03.148_bib19","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/0006-291X(83)91093-8","article-title":"Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H\u20131H spin\u2013spin coupling constants in proteins","volume":"113","author":"Marion","year":"1983","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2009.03.148_bib20","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/S0021-9258(19)41959-5","article-title":"The structure of ferrocytochrome b5 at 2.8 A resolution","volume":"250","author":"Argos","year":"1975","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib21","doi-asserted-by":"crossref","first-page":"3638","DOI":"10.1021\/bi00335a036","article-title":"Axial ligands of chloroplast cytochrome b-559: identification and requirement for a heme-crosslinked polypeptide structure","volume":"24","author":"Babcock","year":"1985","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2009.03.148_bib22","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0076-6879(78)54019-6","article-title":"Circular dichroism spectroscopy of hemoproteins","volume":"54","author":"Myer","year":"1978","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbrc.2009.03.148_bib23","doi-asserted-by":"crossref","first-page":"2940","DOI":"10.1016\/S0021-9258(17)40786-1","article-title":"Magnetic and natural circular dichroism of metalloporphyrin complexes of human and rabbit hemopexin","volume":"253","author":"Morgan","year":"1978","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib24","doi-asserted-by":"crossref","first-page":"4641","DOI":"10.1016\/S0021-9258(19)45035-7","article-title":"The effect of heme binding on the tryptophan residue and the protein conformation of cytochrome b5","volume":"247","author":"Huntley","year":"1972","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib25","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1093\/oxfordjournals.jbchem.a129286","article-title":"Studies of cytochrome b-555 from larvae of the housefly, Musca domestica L. II. Isoelectric point, amino acid composition and circular dichroic spectra","volume":"67","author":"Okada","year":"1970","journal-title":"J. Biochem. (Tokyo)"},{"key":"10.1016\/j.bbrc.2009.03.148_bib26","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/S0021-9258(17)31230-9","article-title":"Purification and some properties of the small subunit of cytochrome b558 from human neutrophils","volume":"264","author":"Yamaguchi","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib27","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1111\/j.1432-1033.1989.tb14796.x","article-title":"Circular dichroic spectroscopy of membrane haemoproteins. The molecular determinants of the dichroic properties of the b cytochromes in various ubiquinol:cytochrome c reductases","volume":"182","author":"Degli Esposti","year":"1989","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib28","unstructured":"G.N. La Mar, J.D. Satterlee, J.S. de Ropp, Nuclear magnetic resonance of hemoproteins, in: K.M. Kadish, K.M. Smith, R. Guilard (Eds.), The Porphyrin Handbook, vol. 5: NMR and EPR, Academic Press, New York, NY, 2000, pp. 185-298."},{"key":"10.1016\/j.bbrc.2009.03.148_bib29","doi-asserted-by":"crossref","unstructured":"F.A. Walker, U. Simonis, Proton NMR spectroscopy of model hemes, in: L.R. Berliner, J. Reuben (Eds.), Biological Magnetic Resonance, vol. 12: NMR of Paramagnetic Molecules, Plenum Press, New York, NY, 1993, pp. 133-274.","DOI":"10.1007\/978-1-4615-2886-9_4"},{"key":"10.1016\/j.bbrc.2009.03.148_bib30","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1007\/s007750050271","article-title":"The effect of axial ligand plane orientation on the contact and pseudocontact shifts of low-spin ferriheme proteins","volume":"3","author":"Shokhirev","year":"1998","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.bbrc.2009.03.148_bib31","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1016\/j.biochi.2003.08.005","article-title":"1H NMR studies of the effect of mutation at Valine45 on heme microenvironment of cytochrome b5","volume":"85","author":"Cao","year":"2003","journal-title":"Biochimie"},{"key":"10.1016\/j.bbrc.2009.03.148_bib32","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1021\/bi971896w","article-title":"The solution structure of oxidized rat microsomal cytochrome b5","volume":"37","author":"Arensano","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2009.03.148_bib33","doi-asserted-by":"crossref","first-page":"8657","DOI":"10.1021\/bi982785f","article-title":"The solution structure of oxidized Escherichia coli cytochrome b562","volume":"38","author":"Arensano","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2009.03.148_bib34","doi-asserted-by":"crossref","first-page":"12988","DOI":"10.1021\/ja063330d","article-title":"Solution 1H NMR characterization of the axial bonding of the two His in oxidized human cytoglobin","volume":"128","author":"Bondarenko","year":"2006","journal-title":"J. Am. Chem. Soc."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X09006482?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X09006482?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,10,3]],"date-time":"2021-10-03T23:24:24Z","timestamp":1633303464000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X09006482"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,5]]},"references-count":34,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2009,5]]}},"alternative-id":["S0006291X09006482"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2009.03.148","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2009,5]]}}}