A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B
dc.contributor.author | Schepler, K. L. | en_US |
dc.contributor.author | Dunham, William Richard | en_US |
dc.contributor.author | Sands, Richard H. | en_US |
dc.contributor.author | Fee, James A. | en_US |
dc.contributor.author | Abeles, R. H. | en_US |
dc.date.accessioned | 2006-04-07T16:35:52Z | |
dc.date.available | 2006-04-07T16:35:52Z | |
dc.date.issued | 1975-08-26 | en_US |
dc.identifier.citation | Schepler, K. L., Dunham, W. R., Sands, R. H., Fee, J. A., Abeles, R. H. (1975/08/26)."A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B." Biochimica et Biophysica Acta (BBA) - Enzymology 397(2): 510-518. <http://hdl.handle.net/2027.42/22002> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GH-47T1W8P-JF/2/2cc4cc1dc16117793d0014f1bea83c10 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22002 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=168925&dopt=citation | en_US |
dc.description.abstract | We have proposed that the "doublet" EPR spectra observed during catalysis by a number of coenzyme B1,2-requiring enzymes arises from a weak electrostatic exchange interaction between an organic free radical and low spin Co(II), B1,2r. By varying the magnitude of the exchange coupling we have quite accurately simulateed the published EPR spectra from the enzyme systems: diol dehydrase, glycerol dehydrase, ribonucleotide reductase, and ethanolamine ammonia lyase. A dipolar model was shown to be incompatible with the observed properties of these systems. | en_US |
dc.format.extent | 521064 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 physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B | 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 | Biophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A. | en_US |
dc.contributor.affiliationum | Biophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A. | en_US |
dc.contributor.affiliationum | Biophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A. | en_US |
dc.contributor.affiliationum | Biophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A. | en_US |
dc.contributor.affiliationum | Biophys Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Mich. 48105; Graduate Department of Biochemistry, Brandeis University, Waltham, Mass. 02154, U.S.A. | en_US |
dc.identifier.pmid | 168925 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22002/1/0000415.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2744(75)90141-2 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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