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dc.contributor.authorPence, Natasha
dc.contributor.authorTokmina-Lukaszewska, Monika
dc.contributor.authorYang, Zhi-Yong
dc.contributor.authorLedbetter, Rhesa N.
dc.contributor.authorSeefeldt, Lance C.
dc.contributor.authorBothner, Brian
dc.contributor.authorPeters, John W.
dc.date.accessioned2018-01-17T19:16:40Z
dc.date.available2018-01-17T19:16:40Z
dc.date.issued2017-08
dc.identifier.citationPence, Natasha, Monika Tokmina-Lukaszewska, Zhi-Yong Yang, Rhesa N. Ledbetter, Lance C. Seefeldt, Brian Bothner, and John W. Peters. "Unraveling the interactions of the physiological reductant flavodoxin with the different conformations of the Fe protein in the nitrogenase cycle." Journal of Biological Chemistry (August 2017): 15661-15669. DOI:https://dx.doi.org/10.1074/jbc.M117.801548.en_US
dc.identifier.issn0021-9258
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/14137
dc.description.abstractNitrogenase reduces dinitrogen (N2) to ammonia in biological nitrogen fixation. The nitrogenase Fe protein cycle involves a transient association between the reduced, MgATP-bound Fe protein and the MoFe protein and includes electron transfer, ATP hydrolysis, release of Pi , and dissociation of the oxidized, MgADP-bound Fe protein from the MoFe protein. The cycle is completed by reduction of oxidized Fe protein and nucleotide exchange. Recently, a kinetic study of the nitrogenase Fe protein cycle involving the physiological reductant flavodoxin reported a major revision of the rate-limiting step from MoFe protein and Fe protein dissociation, to release of Pi . Since the Fe protein cannot interact with flavodoxin and the MoFe protein simultaneously, knowledge of the interactions between flavodoxin and the different nucleotide states of the Fe protein is critically important for understanding the Fe protein cycle. Here, we used time-resolved limited proteolysis and chemical cross-linking to examine nucleotide-induced structural changes in the Fe protein and their effects on interactions with flavodoxin. Differences in proteolytic cleavage patterns and chemical cross-linking patterns were consistent with known nucleotide-induced structural differences in the Fe protein and indicated that MgATP-bound Fe protein resembles the structure of the Fe protein in the stabilized nitrogenase complex structures. Docking models and cross-linking patterns between the Fe protein and flavodoxin revealed that the MgADP-bound state of the Fe protein has the most complementary docking interface with flavodoxin compared with the MgATP-bound state. Together, these findings provide new insights into the control mechanisms in protein-protein interactions during the Fe protein cycle.en_US
dc.rightsThis research was originally published in the Journal of Biological Chemistry. Author(s). Title. J. Biol. Chem. Year; Vol:pp-pp. © the American Society for Biochemistry and Molecular Biology.en_US
dc.titleUnraveling the interactions of the physiological reductant flavodoxin with the different conformations of the Fe protein in the nitrogenase cycleen_US
mus.citation.extentfirstpage15661en_US
mus.citation.extentlastpage15669en_US
mus.citation.journaltitleJournal of Biological Chemistryen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1074/jbc.M117.801548en_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage2en_US


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