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dc.contributor.authorKrishnan, Sadagopan
dc.contributor.authorAbeykoon, Amila
dc.contributor.authorSchenkman, John B
dc.contributor.authorRusling, James F
dc.date.accessioned2018-09-20T16:13:34Z
dc.date.available2018-09-20T16:13:34Z
dc.date.issued2009-11-11
dc.identifier.citationKrishnan, Sadagopan; Abeykoon, Amila; Schenkman, John B; Rusling, James F (2009). Control of electrochemical and ferryloxy formation kinetics of cyt p450s in polyion films by heme iron spin state and secondary structure. Journal of the American Chemical Society 131 (44), 16215-16224
dc.identifier.issn0002-7863,1520-5126
dc.identifier.urihttp://hdl.handle.net/10379/12319
dc.description.abstractVoltammetry of cytochrome P450 (cyt P450) enzymes in ultrathin films with polyions was related for the first time to electronic and secondary structure. Heterogeneous electron transfer (hET) rate constants for reduction of the cyt P450s depended on heme iron spin state, with low spin cyt P450cam giving a value 40-fold larger than high spin human cyt P450 1A2, with mixed spin human P450 cyt 2E1 at an intermediate value. Asymmetric reduction-oxidation peak separations with increasing scan rates were explained by simulations featuring faster oxidation than reduction. Results are consistent with a square scheme in which oxidized and reduced forms of cyt P450s each participate in rapid conformational equilibria. Rate constants for oxidation of ferric cyt P450s in films by t-butyl hydroperoxide to active ferryloxy cyt P450s from rotating disk voltammetry suggested a weaker dependence on spin state, but in the reverse order of the observed hET reduction rates. Oxidation and reduction rates of cyt P450s in the films are also likely to depend on protein secondary structure around the heme iron.
dc.publisherAmerican Chemical Society (ACS)
dc.relation.ispartofJournal of the American Chemical Society
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Ireland
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/3.0/ie/
dc.subjecthuman cytochrome-p450 2e1
dc.subjectbiomembrane-like films
dc.subjectelectron-transfer
dc.subjectcatalytic-activities
dc.subjectescherichia-coli
dc.subjectcrystal-structure
dc.subjectDNA-damage
dc.subjectmyoglobin
dc.subjectp450(cam)
dc.subjectvoltammetry
dc.titleControl of electrochemical and ferryloxy formation kinetics of cyt p450s in polyion films by heme iron spin state and secondary structure
dc.typeArticle
dc.identifier.doi10.1021/ja9065317
dc.local.publishedsourcehttp://europepmc.org/articles/pmc3576030?pdf=render
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Attribution-NonCommercial-NoDerivs 3.0 Ireland
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