Mossbauer spectroscopy applied to the oxidized and semi-reduced states of the iron-molybdenum cofactor of nitrogenase
dc.contributor.author | Newton, William E. | en_US |
dc.contributor.author | Gheller, Stephen F. | en_US |
dc.contributor.author | Sands, Richard H. | en_US |
dc.contributor.author | Dunham, William Richard | en_US |
dc.date.accessioned | 2006-04-07T20:45:18Z | |
dc.date.available | 2006-04-07T20:45:18Z | |
dc.date.issued | 1989-07-31 | en_US |
dc.identifier.citation | Newton, William E., Gheller, Stephen F., Sands, Richard H., Dunham, W. R. (1989/07/31)."Mossbauer spectroscopy applied to the oxidized and semi-reduced states of the iron-molybdenum cofactor of nitrogenase." Biochemical and Biophysical Research Communications 162(2): 882-891. <http://hdl.handle.net/2027.42/27843> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WBK-4DXRXVK-CC/2/811c623353f9265dfee590e9d346a5ed | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/27843 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2757645&dopt=citation | en_US |
dc.description.abstract | Mossbauer parameters at 125K for both the oxidized and semi-reduced states of FeMoco isolated from the MoFe protein of nitrogenase of [delta]/Fe=0.32 and 0.37 mm/s and [Delta]Eq=0.84 and 0.71 mm/s, respectively, are reported. FeMoco(ox) fits the Debye model perfectly from 4.2-125K and has a S=0 ground state. FeMoco(ox) apparently contains 10-20% FeMoco(s-r) and , possibly as a result of the spontaneous oxidation phenomenon. Quantitation of the spectra indicates a Fe:Mo ratio of 5+/-1:1 and the similar quadrupole splittings and isomer shifts suggest a similar environment for all iron atoms. | en_US |
dc.format.extent | 592050 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 | Mossbauer spectroscopy applied to the oxidized and semi-reduced states of the iron-molybdenum cofactor 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, University of Michigan, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationother | Western Regional Research Center, USDA-ARS, Albany, CA 94710, USA; Department of Agronomy and Range Science, University of California, Davis, CA 95616, USA. | en_US |
dc.contributor.affiliationother | Department of Agronomy and Range Science, University of California, Davis, CA 95616, USA; Western Regional Research Center, USDA-ARS, Albany, CA 94710, USA. | en_US |
dc.identifier.pmid | 2757645 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/27843/1/0000253.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-291X(89)92392-9 | en_US |
dc.identifier.source | Biochemical and Biophysical Research Communications | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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