Transport and utilization of rhizoferrin bound iron in Mycobacterium smegmatis
Transport and metabolization of iron bound to the fungal siderophore rhizoferrin was analyzed by transport kinetics, Mössbauer and EPR spectroscopy. Saturation kinetics (vmax = 24.4 pmol/(mg min), K(m) = 64.4 microM) and energy dependence excluded diffusion and provided evidence for a rhizoferrin tr...
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| Veröffentlicht in: | Biometals 1999-12, Vol.12 (4), p.315-321 |
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| creator | Matzanke, B F Böhnke, R Möllmann, U Schünemann, V Schumann, G Trautwein, A X Winkelmann, G |
| description | Transport and metabolization of iron bound to the fungal siderophore rhizoferrin was analyzed by transport kinetics, Mössbauer and EPR spectroscopy. Saturation kinetics (vmax = 24.4 pmol/(mg min), K(m) = 64.4 microM) and energy dependence excluded diffusion and provided evidence for a rhizoferrin transport system in M. smegmatis. Based on the spectroscopic techniques indications for intracellular presence of the ferric rhizoferrin complex were found. This feature could be of practical importance in the search of novel drugs for the treatment of mycobacterial infections. EPR and Mössbauer spectroscopy revealed different ferritin mineral cores depending on the siderophore iron source. This finding was interpreted in terms of different protein shells, i.e. two types of ferritins. |
| doi_str_mv | 10.1023/A:1009274415607 |
| format | Article |
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Saturation kinetics (vmax = 24.4 pmol/(mg min), K(m) = 64.4 microM) and energy dependence excluded diffusion and provided evidence for a rhizoferrin transport system in M. smegmatis. Based on the spectroscopic techniques indications for intracellular presence of the ferric rhizoferrin complex were found. This feature could be of practical importance in the search of novel drugs for the treatment of mycobacterial infections. EPR and Mössbauer spectroscopy revealed different ferritin mineral cores depending on the siderophore iron source. 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Academic</collection><jtitle>Biometals</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matzanke, B F</au><au>Böhnke, R</au><au>Möllmann, U</au><au>Schünemann, V</au><au>Schumann, G</au><au>Trautwein, A X</au><au>Winkelmann, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transport and utilization of rhizoferrin bound iron in Mycobacterium smegmatis</atitle><jtitle>Biometals</jtitle><addtitle>Biometals</addtitle><date>1999-12-01</date><risdate>1999</risdate><volume>12</volume><issue>4</issue><spage>315</spage><epage>321</epage><pages>315-321</pages><issn>0966-0844</issn><eissn>1572-8773</eissn><abstract>Transport and metabolization of iron bound to the fungal siderophore rhizoferrin was analyzed by transport kinetics, Mössbauer and EPR spectroscopy. Saturation kinetics (vmax = 24.4 pmol/(mg min), K(m) = 64.4 microM) and energy dependence excluded diffusion and provided evidence for a rhizoferrin transport system in M. smegmatis. Based on the spectroscopic techniques indications for intracellular presence of the ferric rhizoferrin complex were found. This feature could be of practical importance in the search of novel drugs for the treatment of mycobacterial infections. EPR and Mössbauer spectroscopy revealed different ferritin mineral cores depending on the siderophore iron source. This finding was interpreted in terms of different protein shells, i.e. two types of ferritins.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>10816731</pmid><doi>10.1023/A:1009274415607</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biometals, 1999-12, Vol.12 (4), p.315-321 |
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| subjects | Bacteria Electron Spin Resonance Spectroscopy Ferric Compounds - metabolism Iron Iron - metabolism Kinetics Mycobacterium smegmatis Mycobacterium smegmatis - metabolism Siderophores - metabolism Spectroscopy Spectroscopy, Mossbauer Spectrum analysis |
| title | Transport and utilization of rhizoferrin bound iron in Mycobacterium smegmatis |
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