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On the structure and function of nitrogenase from W5
dc.contributor.authorZumft, Walter G.en_US
dc.contributor.authorCretney, Walter C.en_US
dc.contributor.authorHuang, T. C.en_US
dc.contributor.authorMortenson, Leonard E.en_US
dc.contributor.authorPalmer, Grahamen_US
dc.date.accessioned2006-04-17T16:46:26Z
dc.date.available2006-04-17T16:46:26Z
dc.date.issued1972-09-26en_US
dc.identifier.citationZumft, W. G., Cretney, W. C., Huang, T. C., Mortenson, L. E., Palmer, G. (1972/09/26)."On the structure and function of nitrogenase from W5." Biochemical and Biophysical Research Communications 48(6): 1525-1532. <http://hdl.handle.net/2027.42/34037>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DPC601-9N/2/4bb0ad43559a7e5dc0f6d5058f01a974en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/34037
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4342714&dopt=citationen_US
dc.description.abstractMolybdoferredoxin from W5 was fractionated into MoFd with two atoms of molybdenum per 220,000 daltons and a specific activity of 2.6 [mu]moles C2H2 reduced/min/mg protein and into a catalytically inactive species with an identical protein moiety but an incomplete active centre. Native MoFd is a tetramer composed of two 50,000 and two 60,000 dalton subunits. At low protein concentrations the tetramer is in equilibrium with a dimer. Under low ionic strength and at low pH further dissociation into monomers occurs. MoFd and azoferredoxin have distinct electron paramagnetic resonance spectra. The EPR spectrum of AzoFd and that of the combination of the two nitrogenase components undergoes characteristic changes upon addition of MgATP2-.en_US
dc.format.extent395133 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleOn the structure and function of nitrogenase from W5en_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich., USA; Department of Biological Chemistry, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich., USAen_US
dc.contributor.affiliationotherDepartment of Biological Sciences, Purdue University, Lafayette, Indiana, USAen_US
dc.contributor.affiliationotherDepartment of Biological Sciences, Purdue University, Lafayette, Indiana, USAen_US
dc.contributor.affiliationotherDepartment of Biological Sciences, Purdue University, Lafayette, Indiana, USAen_US
dc.contributor.affiliationotherDepartment of Biological Sciences, Purdue University, Lafayette, Indiana, USAen_US
dc.identifier.pmid4342714en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/34037/1/0000314.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(72)90887-Xen_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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