Electron transfer and redox chemistry in hexa-coordinate hemoglobins

dc.contributor.advisor Mark Hargrove
dc.contributor.author Singh, Navjot
dc.contributor.department Biochemistry, Biophysics and Molecular Biology
dc.date 2018-08-11T07:37:27.000
dc.date.accessioned 2020-06-30T03:02:13Z
dc.date.available 2020-06-30T03:02:13Z
dc.date.copyright Fri Jan 01 00:00:00 UTC 2016
dc.date.embargo 2001-01-01
dc.date.issued 2016-01-01
dc.description.abstract <p>The heme prosthetic group can be held into proteins in a variety of ways. Most often amino acid side chains coordinate one or both of the two available axial coordination sites of the heme iron. Coordination of both sites, such as in cytochrome b5, produces a good electron transfer protein but excludes the binding of exogenous ligands. In hemoglobins, coordination can occur at a single site (as in the “pentacoordinate” hemoglobins associated with oxygen transport), or at both sites (as in the “hexacoordinate” hemoglobins found in a wider distribution of organisms and functions). Surprisingly, hexacoordination in hemoglobins is usually reversible and a variety of exogenous ligands can bind most hexacoordinate hemoglobins. Reversible coordination brings a variety of chemical features to hexacoordinate hemoglobins by affecting their affinity for ligands, redox equilibrium, and the kinetics and extent of electron transfer. These reactions are reviewed for hexa- and pentacoordinate hemoglobins with the goal of using these characteristics for understanding potential functions of hexacoordinate hemoglobins in different species.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/etd/15208/
dc.identifier.articleid 6215
dc.identifier.contextkey 8943328
dc.identifier.doi https://doi.org/10.31274/etd-180810-4808
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath etd/15208
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/29391
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/etd/15208/Singh_iastate_0097E_15711.pdf|||Fri Jan 14 20:37:36 UTC 2022
dc.subject.disciplines Biochemistry
dc.subject.keywords Biochemistry
dc.title Electron transfer and redox chemistry in hexa-coordinate hemoglobins
dc.type article
dc.type.genre dissertation
dspace.entity.type Publication
relation.isOrgUnitOfPublication faf0a6cb-16ca-421c-8f48-9fbbd7bc3747
thesis.degree.discipline Biochemistry
thesis.degree.level dissertation
thesis.degree.name Doctor of Philosophy
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