Hydrocarbon oxidation by a bacterial enzyme system : I. Products of octane oxidation
dc.contributor.author | Baptist, James N. | en_US |
dc.contributor.author | Gholson, Robert K. | en_US |
dc.contributor.author | Coon, Minor J. | en_US |
dc.date.accessioned | 2006-04-13T14:52:21Z | |
dc.date.available | 2006-04-13T14:52:21Z | |
dc.date.issued | 1963 | en_US |
dc.identifier.citation | Baptist, James N., Gholson, Robert K., Coon, Minor J. (1963)."Hydrocarbon oxidation by a bacterial enzyme system : I. Products of octane oxidation." Biochimica et Biophysica Acta 69(): 40-47. <http://hdl.handle.net/2027.42/32244> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73G9-4894KF2-BW/2/8f1b9da196e30ae4e7905d285962ff79 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32244 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=13966404&dopt=citation | en_US |
dc.description.abstract | A Pseudomonad which grows on hexane as sole carbon source was isolated from soil by enrichment-culture technique. Cell-free, soluble enzyme preparations of the organism catalyze the oxidation of 14C-labeled octane to radioactive octanoic acid. A pyridine nucleotide is required for this overall conversion in charcoal-treated bacterial extracts. n-Octanol and octaldehyde were identified as products of octane oxidation and the presence in the enzyme preparations of DPN-dependent dehydrogenases acting on octanol and octaldehyde was demonstrated. | en_US |
dc.format.extent | 862108 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 | Hydrocarbon oxidation by a bacterial enzyme system : I. Products of octane oxidation | 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 | Department of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Mich., U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Mich., U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Mich., U.S.A. | en_US |
dc.identifier.pmid | 13966404 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32244/1/0000306.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-3002(63)91223-X | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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