The iron electron-nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida
dc.contributor.author | Fritz, J. | en_US |
dc.contributor.author | Anderson, R. | en_US |
dc.contributor.author | Fee, James A. | en_US |
dc.contributor.author | Palmer, Graham | en_US |
dc.contributor.author | Sands, Richard H. | en_US |
dc.contributor.author | Tsibris, J. C. M. | en_US |
dc.contributor.author | Gunsalus, I. C. | en_US |
dc.contributor.author | Orme-Johnson, W. H. | en_US |
dc.contributor.author | Beinert, Helmut | en_US |
dc.date.accessioned | 2006-04-17T16:21:12Z | |
dc.date.available | 2006-04-17T16:21:12Z | |
dc.date.issued | 1971-11-02 | en_US |
dc.identifier.citation | Fritz, J., Anderson, R., Fee, J., Palmer, G., Sands, R. H., Tsibris, J. C. M., Gunsalus, I. C., Orme-Johnson, W. H., Beinert, H. (1971/11/02)."The iron electron-nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida." Biochimica et Biophysica Acta (BBA) - Bioenergetics 253(1): 110-133. <http://hdl.handle.net/2027.42/33533> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1S-47PNWH7-131/2/c63c51dadb3b099abffcef410f02689c | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/33533 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4331268&dopt=citation | en_US |
dc.description.abstract | The iron electron-nuclear double resonance (ENDOR) spectra of reduced iron-sulfur proteins (two-iron ferredoxins) from spinach, parsley, pig adrenal cortex and Pseudomonas putida unequivocally show two inequivalent iron atoms at the active sites of each of these proteins. The frequencies of the ENDOR lines establish the total electronic spin in the ground state to be . The principal values of the hyperfine tensor have been determined for each of the iron atoms and these values are consistent with and lend considerable support to the model of a high-spin Fe(III) atom and a high-spin Fe(II) atom antiferromagnetically coupled to form an system. The measured principal axis components of the effective hyperfine tensors for are as follows (1 and 2 refer to the inequivalent iron sites): These data are consistent with Site 1 being ferric and Site 2, ferrous iron. The primes indicate that the A-tensor principal axes for Site 1 (Fe(III)) are apparently rotated about the x-axis with respect to the g-tensor axes by an angle [theta] (20[deg] [les] [theta] [les] 40[deg]). The orientations of the A-tensors for Site 2 (Fe(II)) have not been determined and hence the values presented are the observed values of the A-tensors along the x, y, and z-axes of the g-tensor for this complex.A brief introduction to the theory of ENDOR is given. | en_US |
dc.format.extent | 1382410 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 | The iron electron-nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | 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, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Biochemistry, University of Illinois, Urbana, Ill. 61801, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Biochemistry, University of Illinois, Urbana, Ill. 61801, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Biochemistry and Institute for Enzyme Research, University of Wisconsin, Madison, Wisc. 53706, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Biochemistry and Institute for Enzyme Research, University of Wisconsin, Madison, Wisc. 53706, U.S.A. | en_US |
dc.identifier.pmid | 4331268 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/33533/1/0000032.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2728(71)90239-8 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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