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On the prosthetic group(s) of component II from nitrogenase : EPR of the Fe-protein from Azotobacter vinelandii
dc.contributor.authorHagen, Wilfred R.en_US
dc.contributor.authorDunham, William Richarden_US
dc.contributor.authorBraaksma, Arnolden_US
dc.contributor.authorHaaker, Huuben_US
dc.date.accessioned2006-04-07T19:02:23Z
dc.date.available2006-04-07T19:02:23Z
dc.date.issued1985-07-22en_US
dc.identifier.citationHagen, W. R., Dunham, W. R., Braaksma, A., Haaker, H. (1985/07/22)."On the prosthetic group(s) of component II from nitrogenase : EPR of the Fe-protein from Azotobacter vinelandii." FEBS Letters 187(1): 146-150. <http://hdl.handle.net/2027.42/25617>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T36-44PFR41-13/2/5e220a5933041bbd0d3dc7b83eb6db51en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/25617
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2991004&dopt=citationen_US
dc.description.abstractThe EPR spectrum of the reduced Fe-protein from nitrogenase has been reinvestigated. The dependences on temperature, microwave power, and microwave frequency all suggest that the observed signal represents a magnetically isolated [4Fe-4S]1+(2+;1+) cluster. Also, the signal can be simulated assuming a simple, gstrained S = system. However, the integrated intensity amounts to no more than 0.2 spins per protein molecule. It is, therefore, impossible that Fe-protein preparations contain a single type of [4Fe-4S] cluster.en_US
dc.format.extent508171 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleOn the prosthetic group(s) of component II from nitrogenase : EPR of the Fe-protein from Azotobacter vinelandiien_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, The University of Michigan, Ann Arbor, MI 48109, USAen_US
dc.contributor.affiliationotherDepartment ofBiochemistry, Agricultural University, De Dreijen 11, 6703 BC Wageningen, The Netherlandsen_US
dc.contributor.affiliationotherDepartment ofBiochemistry, Agricultural University, De Dreijen 11, 6703 BC Wageningen, The Netherlandsen_US
dc.contributor.affiliationotherDepartment ofBiochemistry, Agricultural University, De Dreijen 11, 6703 BC Wageningen, The Netherlandsen_US
dc.identifier.pmid2991004en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/25617/1/0000165.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0014-5793(85)81231-Xen_US
dc.identifier.sourceFEBS Lettersen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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