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dc.creatorPopovic, DM
dc.creatorZarić, Snežana D.
dc.creatorRabenstein, B
dc.creatorKnapp, EW
dc.date.accessioned2018-11-22T00:03:52Z
dc.date.available2018-11-22T00:03:52Z
dc.date.issued2001
dc.identifier.issn0002-7863
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/459
dc.description.abstractWe generated atomic coordinates of an artificial protein that was recently synthesized to model the central part of the native cytochrome b (Cb) subunit consisting of a four-helix bundle with two hemes. Since no X-ray structure is available, the structural elements of the artificial Cb were assembled from scratch using all known chemical and structural information available and avoiding strain as much as possible. Molecular dynamics (MD) simulations applied to this model protein exhibited root-mean-square deviations as small as those obtained from MD simulations starting with the crystal structure of the native Cb subunit. This demonstrates that the modeled structure of the artificial Cb is relatively rigid and strain-free. The model structure of the artificial Cb was used to determine the redox potentials of the two hemes by calculating the electrostatic energies from the solution of the linearized Poisson-Boltzmann equation (LPBE). The calculated redox potentials agree within 20 meV with the experimentally measured values. The dependence of the redox potentials of the hemes on the protein environment was analyzed. Accordingly, the total shift in the redox potentials is mainly due to the low dielectric medium of the protein, the protein backbone charges, and the salt bridges formed between the arginines and the propionic acid groups of the hemes. The difference in the shift of the redox potentials is due to the interactions with the hydrophilic side chains and the salt bridges formed with the propionic acids of the hemes. For comparison and to test the computational procedure, the redox potentials of the two hemes in the native Cb from the cytochrome bc(1) (Cbc(1)) complex were also calculated. Also in this case the computed redox potentials agree well with experiments.en
dc.publisherAmer Chemical Soc, Washington
dc.rightsrestrictedAccess
dc.sourceJournal of the American Chemical Society
dc.titleArtificial cytochrome b: Computer modeling and evaluation of redox potentialsen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractКнапп, ЕW; Зарић, Снежана; Рабенстеин, Б; Поповиц, ДМ;
dc.citation.volume123
dc.citation.issue25
dc.citation.spage6040
dc.citation.epage6053
dc.identifier.wos000169534000021
dc.identifier.doi10.1021/ja003878z
dc.citation.other123(25): 6040-6053
dc.citation.rankaM21
dc.identifier.pmid11414837
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-0034832979
dc.identifier.rcubKon_1433


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