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Characterization of the [omega]-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein

dc.contributor.authorRuettinger, Richard T.en_US
dc.contributor.authorGriffith, Gary R.en_US
dc.contributor.authorCoon, Minor J.en_US
dc.date.accessioned2006-04-07T17:08:31Z
dc.date.available2006-04-07T17:08:31Z
dc.date.issued1977-10en_US
dc.identifier.citationRuettinger, Richard T., Griffith, Gary R., Coon, Minor J. (1977/10)."Characterization of the [omega]-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein." Archives of Biochemistry and Biophysics 183(2): 528-537. <http://hdl.handle.net/2027.42/22832>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DYTNJ1-DD/2/0091b5ef5b065772ba01cd5cfc9d9993en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/22832
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=921275&dopt=citationen_US
dc.description.abstractThe [omega]-hydroxylase of Pseudomonas oleovorans, which catalyzes the hydroxylation of fatty acids and alkanes and the epoxidation of alkenes in the presence of a reduced pyridine nucleotide, a reductase, rubredoxin, and molecular oxygen, has been purified to electrophoretic homogeneity. Octane hydroxylation and octadiene epoxidation activities appear to remain at a constant ratio during the purification procedure. The hydroxylase has been characterized as a nonheme iron protein containing one iron atom and one cysteine residue per polypeptide chain of molecular weight 40,800. The enzyme is inhibited by cyanide, and activity is restored upon removal of the cyanide by dialysis. Iron is removed from the enzyme by dialysis against EDTA provided that a reducing agent such as dithionite or ascorbate is also added, and enzyme activity is restored by the addition of ferrous ions to the apohydroxylase.en_US
dc.format.extent1121133 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleCharacterization of the [omega]-hydroxylase of Pseudomonas oleovorans as a nonheme iron proteinen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.identifier.pmid921275en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/22832/1/0000392.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(77)90388-5en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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