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dc.contributor.authorGarcia Costas, Amaya M.
dc.contributor.authorPoudel, Saroj
dc.contributor.authorMiller, Anne-Frances
dc.contributor.authorSchut, Gerrit J.
dc.contributor.authorLedbetter, Rhesa N.
dc.contributor.authorFixen, Kathryn R.
dc.contributor.authorSeefeldt, Lance C.
dc.contributor.authorAdams, Michael W. W.
dc.contributor.authorHarwood, Caroline S.
dc.contributor.authorBoyd, Eric S.
dc.contributor.authorPeters, John W.
dc.date.accessioned2018-03-13T17:41:22Z
dc.date.available2018-03-13T17:41:22Z
dc.date.issued2017-11
dc.identifier.citationGarcia Costas, Amaya M, Saroj Poudel, Anne-Frances Miller, Gerrit J Schut, Rhesa N Ledbetter, Kathryn R Fixen, Lance C Seefeldt, Michael W W Adams, Caroline S Harwood, Eric S Boyd, and John W Peters. "Defining Electron Bifurcation in the Electron Transferring Flavoprotein Family." Journal of Bacteriology 199, no. 21 (November 2017). DOI: 10.1128/JB.00440-17.en_US
dc.identifier.issn1098-5530
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/14462
dc.description.abstractElectron bifurcation is the coupling of exergonic and endergonic redox reactions to simultaneously generate (or utilize) low and high potential electrons. It is the third recognized form of energy conservation in biology and has recently been described in select electron transferring flavoproteins (Etfs). Etfs are flavin-containing heterodimers best known for donating electrons derived from fatty acid and amino acid oxidation to an electron transfer respiratory chain via ETF quinone oxidoreductase. Canonical examples contain a flavin adenine dinucleotide (FAD) that is involved in electron transfer as well as a non-redox active adenosine monophosphate (AMP). However, Etfs demonstrated to bifurcate electrons contain a second FAD in place of the AMP. To expand our understanding of the functional variety and metabolic significance of Etfs and to identify amino acid sequence motifs that potentially enable electron bifurcation, we compiled 1,314 Etf protein sequences from genome sequence databases and subjected them to informatics and structural analyses. Etfs were identified in diverse archaea and bacteria, and these clustered into five distinct well-supported groups based on amino acid sequences. Gene neighborhood analyses indicate that these Etf group designations largely correspond to putative differences in functionality. Etfs with the demonstrated ability to bifurcate were found to form one group, suggesting distinct and conserved amino acid sequence motifs enable this capability. Indeed, structural modeling and sequence alignments revealed that identifying residues occur in the NADH and FAD-binding regions of bifurcating Etfs. Collectively, a new classification scheme is presented for Etf proteins that demarcates putative bifurcating vs. non-bifurcating members and suggests that Etf mediated bifurcation is associated with surprisingly diverse enzymes.IMPORTANCE Electron bifurcation has recently been recognized as an electron transfer mechanism used by microorganisms to maximize energy conservation. Bifurcating enzymes couple thermodynamically unfavorable reactions with thermodynamically favorable reactions in an overall spontaneous process. Here we show that the electron transferring flavoprotein (Etf) enzyme family exhibits far greater diversity than previously recognized and we provide a phylogenetic analysis that clearly delineates bifurcating and non-bifurcating members of this family. Structural modeling of proteins within these groups reveals key differences between the bifurcating and non-bifurcating Etfs.en_US
dc.description.sponsorshipU.S. Department of Energy; Office of Science; Basic Energy Sciences DE-SC0012518en_US
dc.titleDefining Electron Bifurcation in the Electron Transferring Flavoprotein Familyen_US
mus.citation.issue21en_US
mus.citation.journaltitleJournal of Bacteriologyen_US
mus.citation.volume199en_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1128/JB.00440-17en_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.thumbpage4en_US
mus.contributor.orcidPeters, John W.|0000-0001-9117-9568en_US


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