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dc.contributor.authorChoi, Dong W.
dc.contributor.authorZea, Corbin J.
dc.contributor.authorDo, Young S.
dc.contributor.authorSemrau, Jeremy D.
dc.contributor.authorAntholine, William E.
dc.contributor.authorHargrove, Mark S.
dc.contributor.authorPohl, Nicola L.
dc.contributor.authorBoyd, Eric S.
dc.contributor.authorGeesey, Gill G.
dc.contributor.authorHartsel, Scott C.
dc.contributor.authorShafe, Peter H.
dc.contributor.authorMcEllistrem, Marcus T.
dc.contributor.authorKisting, Clint J.
dc.contributor.authorCampbell, Damon
dc.contributor.authorRao, Vinay
dc.contributor.authorde la Mora, Arlene
dc.contributor.authorDiSpirito, Alan A.
dc.date.accessioned2017-07-13T22:15:46Z
dc.date.available2017-07-13T22:15:46Z
dc.date.issued2006-02
dc.identifier.citationChoi DW, Zea CJ, Do YS, Semrau JD, Antholine WE, Hargrove MS, Pohl NL, Boyd ES, Geesey GG, Hartsel SC, Shafe PH, McEllistrem MT, Kisting CJ, Campbell D, Rao V, de la Mora AM, DiSpirito AA, "Spectral, kinetic, and thermodynamic properties of Cu(I) and Cu(II) binding by methanobactin from Methylosinus trichosporium OB3b," Biochemistry, 2006 45(5):1442-1453en_US
dc.identifier.issn0006-2960
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/13282
dc.description.abstractTo examine the potential role of methanobactin (mb) as the extracellular component of a copper acquisition system in Methylosinus trichosporium OB3b, the metal binding properties of mb were examined. Spectral (UV-visible, fluorescence, and circular dichroism), kinetic, and thermodynamic data suggested copper coordination changes at different Cu(II):mb ratios. Mb appeared to initially bind Cu(II) as a homodimer with a comparatively high copper affinity at Cu(II):mb ratios below 0.2, with a binding constant (K) greater than that of EDTA (log K ) 18.8) and an approximate ΔG° of -47 kcal/mol. At Cu(II):mb ratios between 0.2 and 0.45, the K dropped to (2.6 ± 0.46) 108 with a ΔG° of -11.46 kcal/mol followed by another K of (1.40 ± 0.21) 106 and a ΔG° of -8.38 kcal/mol at Cu(II):mb ratios of 0.45-0.85. The kinetic and spectral changes also suggested Cu(II) was initially coordinated to the 4-thiocarbonyl-5-hydroxy imidazolate (THI) and possibly Tyr, followed by reduction to Cu(I), and then coordination of Cu(I) to 4-hydroxy-5-thiocarbonyl imidazolate (HTI) resulting in the final coordination of Cu(I) by THI and HTI. The rate constant (kobsI) of binding of Cu(II) to THI exceeded that of the stopped flow apparatus that was used, i.e., >640 s-1, whereas the coordination of copper to HTI showed a 6-8 ms lag time followed by a kobsII of 121 ± 9 s-1. Mb also solubilized and bound Cu(I) with a kobsI to THI of >640 s-1, but with a slower rate constant to HTI (kobsII ) 8.27 ± 0.16 s-1), and appeared to initially bind Cu(I) as a monomer.en_US
dc.titleSpectral, kinetic, and thermodynamic properties of Cu(I) and Cu(II) binding by methanobactin from Methylosinus trichosporium OB3ben_US
dc.typeArticleen_US
mus.citation.extentfirstpage1442en_US
mus.citation.extentlastpage1453en_US
mus.citation.issue5en_US
mus.citation.journaltitleBiochemistryen_US
mus.citation.volume45en_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.doi10.1021/bi051815ten_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentChemical Engineering.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.relation.researchgroupCenter for Biofilm Engineering.en_US
mus.data.thumbpage6en_US


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