A novel S = 3/2 EPR signal associated with native Fe-proteins of nitrogenase
dc.contributor.author | Hagen, Wilfred R. | en_US |
dc.contributor.author | Eady, R. R. | en_US |
dc.contributor.author | Dunham, William Richard | en_US |
dc.contributor.author | Haaker, Huub | en_US |
dc.date.accessioned | 2006-04-07T18:58:35Z | |
dc.date.available | 2006-04-07T18:58:35Z | |
dc.date.issued | 1985-09-23 | en_US |
dc.identifier.citation | Hagen, W. R., Eady, R. R., Dunham, W. R., Haaker, H. (1985/09/23)."A novel S = 3/2 EPR signal associated with native Fe-proteins of nitrogenase." FEBS Letters 189(2): 250-254. <http://hdl.handle.net/2027.42/25566> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T36-451N9JC-N/2/789fec547c080e1c9b6443a3d461d740 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/25566 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2995120&dopt=citation | en_US |
dc.description.abstract | In addition to their g = 1.94 EPR signal, nitrogenase Fe-proteins from Azotobacter vinelandii, Azotobacter chroococcum and Klebsiella pneumoniae exhibit a weak EPR signal with g [congruent with]5. Temperature dependence of the signal was consistent with an S = 3/2 system with negative zero-field splitting, d = -5 +/- 0.7 cm-1. The ms, = +/- 3/2 ground state doublet gives rise to a transition with geff = 5.90 and the transition within the excited ms = +/- 1/2 doublet has a split geff = 4.8, 3.4. Quantitation gave 0.6 to 0.8 spin mol-1 which summed with the spin intensity of the S = 1/2 G = 1.94 line to roughly 1 spin/mol. MgATP and MgADP decreased the intensity of the s = 3/2 signal with no concomitant changes in intensity of the s = 1/2 signal. | en_US |
dc.format.extent | 479979 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | A novel S = 3/2 EPR signal associated with native Fe-proteins of nitrogenase | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology, The University of Michigan, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationother | Department of Biochemistry, Agricultural University, De Dreijen 11, 6703 BC Wageningen, The Netherlands | en_US |
dc.contributor.affiliationother | AFRC Unit of Nitrogen Fixation, University of Sussex, Brighton BN1 9RQ, England | en_US |
dc.contributor.affiliationother | Department of Biochemistry, Agricultural University, De Dreijen 11, 6703 BC Wageningen, The Netherlands | en_US |
dc.identifier.pmid | 2995120 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/25566/1/0000108.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0014-5793(85)81033-4 | en_US |
dc.identifier.source | FEBS Letters | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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