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dc.contributor.authorBerry, Luke
dc.contributor.authorPoudel, Saroj
dc.contributor.authorTokmina-Lukaszewska, Monika
dc.contributor.authorColman, Daniel R.
dc.contributor.authorNguyen, Diep M. N.
dc.contributor.authorSchut, Gerrit J.
dc.contributor.authorAdams, Michael W. W.
dc.contributor.authorPeters, John W.
dc.contributor.authorBoyd, Eric S.
dc.contributor.authorBothner, Brian
dc.date.accessioned2018-07-11T15:19:30Z
dc.date.available2018-07-11T15:19:30Z
dc.date.issued2018-01
dc.identifier.citationBerry, Luke, S Poudel, M Tokmina-Lukaszewska, D.R. Colman, D.M.N. Nguyen, G.J. Schut, M.W.W. Adams, J.W. Peters, Eric S. Boyd, and Brian Bothner. "H/D exchange mass spectrometry and statistical coupling analysis reveal a role for allostery in a ferredoxin-dependent bifurcating transhydrogenase catalytic cycle." BBA - Biochimica et Biophysica Acta 1862, no. 1 (January 2018): 9-17. DOI: 10.1016/j.bbagen.2017.10.002.en_US
dc.identifier.issn0304-4165
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/14634
dc.description.abstractRecent investigations into ferredoxin-dependent transhydrogenases, a class of enzymes responsible for electron transport, have highlighted the biological importance of flavin-based electron bifurcation (FBEB). FBEB generates biomolecules with very low reduction potential by coupling the oxidation of an electron donor with intermediate potential to the reduction of high and low potential molecules. Bifurcating systems can generate biomolecules with very low reduction potentials, such as reduced ferredoxin (Fd), from species such as NADPH. Metabolic systems that use bifurcation are more efficient and confer a competitive advantage for the organisms that harbor them. Structural models are now available for two NADH-dependent ferredoxin-NADP(+) oxidoreductase (Nfn) complexes. These models, together with spectroscopic studies, have provided considerable insight into the catalytic process of FBEB. However, much about the mechanism and regulation of these multi-subunit proteins remains unclear. Using hydrogen/deuterium exchange mass spectrometry (HDX-MS) and statistical coupling analysis (SCA), we identified specific pathways of communication within the model FBEB system, Nfn from Pyrococus furiosus, under conditions at each step of the catalytic cycle. HDX-MS revealed evidence for allosteric coupling across protein subunits upon nucleotide and ferredoxin binding. SCA uncovered a network of co-evolving residues that can provide connectivity across the complex. Together, the HDX-MS and SCA data show that protein allostery occurs across the ensemble of iron-sulfur cofactors and ligand binding sites using specific pathways that connect domains allowing them to function as dynamically coordinated units.en_US
dc.rightsThis Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).en_US
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en_US
dc.titleH/D exchange mass spectrometry and statistical coupling analysis reveal a role for allostery in a ferredoxin-dependent bifurcating transhydrogenase catalytic cycleen_US
dc.typeArticleen_US
mus.citation.extentfirstpage9en_US
mus.citation.extentlastpage17en_US
mus.citation.issue1en_US
mus.citation.journaltitleBBA - General Subjectsen_US
mus.citation.volume1862en_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1016/j.bbagen.2017.10.002en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage3en_US
mus.contributor.orcidBothner, Brian|0000-0003-1295-9609en_US
mus.contributor.orcidPeters, John W.|0000-0001-9117-9568en_US
mus.contributor.orcidTokmina-Lukaszewska, Monika|0000-0003-3298-8298en_US


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