Structure-function studies of the Vitreoscilla hemoglobin D-region
DC Field | Value | Language |
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dc.contributor.author | Lee SY | - |
dc.contributor.author | Stark BC | - |
dc.contributor.author | Webster DA | - |
dc.date.accessioned | 2023-02-07T14:40:07Z | - |
dc.date.available | 2023-02-07T14:40:07Z | - |
dc.date.created | 2023-02-05 | - |
dc.date.issued | 2004-04 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/86839 | - |
dc.description.abstract | The D-region connecting helices C and E of Vitreoscilla hemoglobin (VHb) appears disordered in the crystal structure. Six site-directed mutants in this region were made to investigate its possible functions. The mutant VHb's were analyzed using UV-visible and FTIR spectroscopy, using primarily the CO liganded forms, and their heme/protein ratios were determined. The results implicate Asp44, Arg47. and Glu49 as especially important in heme-globin interactions and ligand binding, and enabled construction of a model in which the D-region forms a loop that protrudes upward over the heme. Interactions between VHb (wild type and the D-region mutants) with the flavin domain of 2,4-DNT dioxygenase from Burkholderia were tested using bacterial two-hybrid screening. There was a correlation between the extent of the D-loop perturbation predicted for each mutant and the amount of the reduction in VHb-flavin domain interaction, suggesting that this region may be more generally involved in binding of VHb to flavoproteins. (C) 2004 Elsevier Inc. All rights reserved. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.title | Structure-function studies of the Vitreoscilla hemoglobin D-region | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000220579300020 | - |
dc.identifier.doi | 10.1016/j.bbrc.2004.02.154 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.316, no.4, pp.1101 - 1106 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.scopusid | 2-s2.0-1642325905 | - |
dc.citation.endPage | 1106 | - |
dc.citation.startPage | 1101 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 316 | - |
dc.citation.number | 4 | - |
dc.contributor.affiliatedAuthor | Lee SY | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | heme-protein interactions | - |
dc.subject.keywordAuthor | bacterial hemoglobin | - |
dc.subject.keywordAuthor | flavin domain | - |
dc.subject.keywordAuthor | hemoglobin-flavoprotein interactions | - |
dc.subject.keywordPlus | SP STRAIN DNT | - |
dc.subject.keywordPlus | BACTERIAL HEMOGLOBIN | - |
dc.subject.keywordPlus | OXYGEN-BINDING | - |
dc.subject.keywordPlus | BURKHOLDERIA | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | INTERMEDIATE | - |
dc.subject.keywordPlus | ENHANCEMENT | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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