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References from Molecular Mechanisms of Bacterial Bioluminescence. Local targets link to admitted publications; unresolved targets remain external evidence.
10.1126/science.1174269
10.1126/science.1174269 · External reference
Unresolved reference
2009 · External reference
10.1146/annurev-marine-120308-081028
10.1146/annurev-marine-120308-081028 · External reference
Biochemistry and physiology of bioluminescent bacteria
10.1016/s0065-2911(08)60398-7 · 1985 · External reference
10.1073/pnas.1116683109
10.1073/pnas.1116683109 · External reference
Unresolved reference
2014 · External reference
10.1128/mr.55.1.123-142.1991
10.1128/mr.55.1.123-142.1991 · External reference
10.1111/j.1574-6941.2010.01004.x
10.1111/j.1574-6941.2010.01004.x · External reference
10.1111/j.1574-6976.2010.00250.x
10.1111/j.1574-6976.2010.00250.x · External reference
10.1128/jb.00101-08
10.1128/jb.00101-08 · External reference
10.1093/nar/gkw408
10.1093/nar/gkw408 · External reference
Evidence for tetradecanal as the natural aldehyde in bacterial bioluminescence
10.1073/pnas.76.1.265 · 1979 · External reference
Bacterial bioluminescence: organization, regulation, and application of the lux genes
10.1096/fasebj.7.11.8370470 · 1993 · External reference
Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction
10.1073/pnas.81.10.2990 · 1984 · External reference
Crystal structure of the bacterial luciferase/flavin complex provides insight into the function of the β subunit
10.1021/bi900003t · 2009 · External reference
The FMN-dependent two-component monooxygenase systems
10.1016/j.abb.2010.02.007 · 2010 · External reference
10.1016/j.jbiotec.2006.03.044
10.1016/j.jbiotec.2006.03.044 · External reference
10.1021/bi982849m
10.1021/bi982849m · External reference
10.1128/jb.176.12.3544-3551.1994
10.1128/jb.176.12.3544-3551.1994 · External reference
10.1006/bbrc.1998.8641
10.1006/bbrc.1998.8641 · External reference
10.1128/jb.01660-07
10.1128/jb.01660-07 · External reference
Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi (TH1): half-sites reactivity
10.1021/bi1009985 · 2010 · External reference
Phylogenetic diversity and cosymbiosis in the bioluminescent symbioses of “Photobacterium mandapamensis”
10.1128/aem.02212-06 · 2007 · External reference
Phylogenetic analysis of the lux operon distinguishes two evolutionarily distinct clades of Photobacterium leiognathi
10.1007/s00203-004-0663-7 · 2004 · External reference
Crystallization of Photobacterium leiognathi non-fluorescent flavoprotein with limited sequence identity to bacterial luciferase
10.1016/0022-2836(92)91015-h · 1992 · External reference
Crystal structure of a flavoprotein related to the subunits of bacterial luciferase
10.1002/j.1460-2075.1993.tb05824.x · 1993 · External reference
Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 Å resolution
10.1006/jmbi.1995.0289 · 1995 · External reference
Structural and biochemical properties of LuxF from Photobacterium leiognathi
10.1016/j.bbapap.2015.07.008 · 2015 · External reference
Evidence for the generation of myristylated FMN by bacterial luciferase
10.1111/mmi.13676 · 2017 · External reference
Strongly enhanced bacterial bioluminescence with the ilux operon for single-cell imaging
10.1073/pnas.1715946115 · 2018 · External reference
Engineering an enhanced, thermostable, monomeric bacterial luciferase gene as a reporter in plant protoplasts
2014 · External reference
Shedding light on bioluminescence regulation in Vibrio fischeri
10.1111/j.1365-2958.2012.08065.x · 2012 · External reference
Quorum sensing and quorum quenching in Vibrio harveyi: lessons learned from in vivo work
10.1038/ismej.2007.92 · 2008 · External reference
Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi
10.1006/bbrc.2001.5013 · 2001 · External reference
The lux genes and riboflavin genes in bioluminescent system of Photobacterium leiognathi are under common regulation
2004 · External reference
A luminous bacterium that emits yellow light
10.1126/science.850787 · 1977 · External reference
Yellow light emission of Vibrio fischeri strain Y-1: purification and characterization of the energy-accepting yellow fluorescent protein
10.1073/pnas.84.24.8912 · 1987 · External reference
10.1016/0006-291x(87)90696-6
10.1016/0006-291x(87)90696-6 · External reference
Separation of a blue fluorescence protein from bacterial luciferase
10.1016/0006-291x(78)91097-5 · 1978 · External reference
Purification of lumazine proteins from Photobacterium leiognathi and Photobacterium phosphoreum: bioluminescence properties
10.1021/bi00327a026 · 1985 · External reference
Spectral properties and function of two lumazine proteins from Photobacterium
10.1021/bi00327a028 · 1985 · External reference
Lumazine protein from the bioluminescent bacterium Photobacterium phosphoreum
10.1016/s0021-9258(18)43574-0 · 1980 · External reference
Separation and structure of the prosthetic group of the blue fluorescence protein from the bioluminescent bacterium Photobacterium phosphoreum
10.1073/pnas.76.7.3068 · 1979 · External reference
Isolation of the in vivo emitter in bacterial bioluminescence
10.1073/pnas.75.2.833 · 1978 · External reference
Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive
10.1021/bi9608931 · 1996 · External reference
A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system: energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1
10.1073/pnas.87.4.1466 · 1990 · External reference
Unresolved reference
1986 · External reference
10.1007/s13238-011-1118-y
10.1007/s13238-011-1118-y · External reference
Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1
10.1021/bi952691v · 1996 · External reference
Structure of lumazine protein, an optical transponder of luminescent bacteria
10.1016/j.jmb.2008.06.052 · 2008 · External reference
Crystal structures of the lumazine protein from Photobacterium kishitanii in complexes with the authentic chromophore, 6,7-dimethyl-8-(1′-D-ribityl) lumazine, and its analogues, riboflavin and flavin mononucleotide, at high resolution
10.1128/jb.01015-09 · 2010 · External reference
Lumazine protein and the excitation mechanism in bacterial bioluminescence
10.1016/0301-4622(93)85006-4 · 1993 · External reference
10.1142/6102
10.1142/6102 · 2006 · External reference
10.4159/harvard.9780674068025
10.4159/harvard.9780674068025 · 2013 · External reference
10.1089/15230860152665046 · 2001 · Admitted local publication
Flavogenomics - a genomic and structural view of flavin-dependent proteins
10.1111/j.1742-4658.2011.08202.x · 2011 · External reference
Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution
10.1021/bi00020a002 · 1995 · External reference
The 1.5 Å resolution crystal structure of bacterial luciferase in low salt conditions
10.1074/jbc.271.36.21956 · 1996 · External reference
The oxygenated bacterial luciferase-flavin intermediate. Reaction products via the light and dark pathways
10.1016/s0021-9258(19)40942-3 · 1975 · External reference
Spectral properties of an oxygenated luciferase-flavin intermediate isolated by low-temperature chromatography
10.1073/pnas.70.12.3468 · 1973 · External reference
Boronic acids as mechanistic probes for the bacterial luciferase reaction
10.1111/j.1751-1097.1991.tb02019.x · 1991 · External reference
Identifications of the true carbon-13 nuclear magnetic resonance spectrum of the stable intermediate II in bacterial luciferase
10.1021/bi00372a040 · 1986 · External reference
10.1016/j.abb.2009.11.028
10.1016/j.abb.2009.11.028 · External reference
Bioluminophore and flavin mononucleotide fluorescence quenching of bacterial bioluminescence—a theoretical study
10.1002/chem.201603314 · 2016 · External reference
Spectral detection of an intermediate preceding the excited state in the bacterial luciferase reaction
10.1021/bi00214a017 · 1993 · External reference
Bacterial luciferase. Binding of oxidized flavin mononucleotide
10.1016/s0021-9258(19)41555-x · 1975 · External reference
Understanding bacterial bioluminescence: a theoretical study of the entire process, from reduced flavin to light emission
10.1002/chem.201400253 · 2014 · External reference
Unresolved reference
2013 · External reference
A postulated mechanism for the bioluminescent oxidation of reduced flavin mononucleotide
10.1016/0006-291x(72)90719-x · 1972 · External reference
Functional group diversity in enzymatic oxygenation reactions catalyzed by bacterial flavin-containing cyclohexanone oxygenase
10.1021/ja00293a054 · 1985 · External reference
Mechanism of bacterial bioluminescence: 4a,5-dihydroflavin analogs as models for luciferase hydroperoxide intermediates and the effect of substituents at the 8-position of flavin on luciferase kinetics
10.1021/bi00053a004 · 1993 · External reference
Properties of 4a-hydroxy-4a,5-dihydroflavin radicals in relation to bacterial bioluminescence
10.1021/j100204a074 · 1992 · External reference
Deuterium kinetic isotope effects and the mechanism of the bacterial luciferase reaction
10.1021/bi972266x · 1998 · External reference
Chemiluminescence of organic peroxides. Conversion of ground-state reactants to excited-state products by the chemically initiated electron-exchange luminescence mechanism
10.1021/ar50142a003 · 1979 · External reference
Bacterial bioluminescence: spectral study of the emitters in the in vitro reaction
10.1073/pnas.78.2.948 · 1981 · External reference
Bioluminescence of the firefly: key steps in the formation of the electronically excited state for model systems
1978 · External reference
Electron transfer and chemiluminescence. Two inefficient systems: 1,4-dimethoxy-9,10-diphenylanthracene peroxide and diphenoyl peroxide
10.1021/ja00189a043 · 1989 · External reference
Bioluminescence of firefly squid via mechanism of single electron-transfer oxygenation and charge-transfer-induced luminescence
2017 · External reference
Mechanistic insight into the chemiluminescent decomposition of firefly dioxetanone
2012 · External reference
The theoretical estimation of the bioluminescent efficiency of the firefly via a nonadiabatic molecular dynamics simulation
2015 · External reference
Mechanistic insight into Cypridina bioluminescence with a combined experimental and theoretical chemiluminescent approach
10.1021/acs.jpcb.7b06295 · 2017 · External reference
Theoretically obtained insight into the mechanism and dioxetanone species responsible for the singlet chemiexcitation of Coelenterazine
2017 · External reference
Unresolved reference
1978 · External reference
Unresolved reference
1987 · External reference
Differential transfers of reduced flavin cofactor and product by bacterial flavin reductase to luciferase
10.1021/bi0024310 · 2001 · External reference
The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion
10.1021/bi4006545 · 2013 · External reference
Fre is the major flavin reductase supporting bioluminescence from Vibrio harveyi luciferase in Escherichia coli
10.1074/jbc.m808977200 · 2009 · External reference
10.1016/s0021-9258(18)98772-7
10.1016/s0021-9258(18)98772-7 · External reference
Generation of fatty acids by an acyl esterase in the bioluminescent system of Photobacterium phosphoreum
10.1016/s0021-9258(18)90952-x · 1984 · External reference
Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi
10.1021/bi00198a003 · 1994 · External reference
Subunit structure of the fatty acid reductase complex from Photobacterium phosphoreum
10.1021/bi00363a021 · 1986 · External reference
Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria
10.1016/0022-2836(91)90858-4 · 1991 · External reference
10.1016/j.str.2015.08.012
10.1016/j.str.2015.08.012 · External reference
Defining a structural and kinetic rationale for paralogous copies of phenylacetate-CoA ligases from the cystic fibrosis pathogen Burkholderia cenocepacia J2315
10.1074/jbc.m111.219683 · 2011 · External reference
SWISS-MODEL: modeling protein tertiary and quaternary structure using evolutionary information
10.1093/nar/gku340 · 2014 · External reference
Intersubunit transfer of fatty acyl groups during fatty acid reduction
10.1016/s0021-9258(18)66663-3 · 1986 · External reference
Cysteine-286 as the site of acylation of the Lux-specific fatty acyl-CoA reductase
10.1016/s0167-4838(96)00203-8 · 1997 · External reference
Purification of the acyl coenzyme A reductase component from a complex responsible for the reduction of fatty acids in bioluminescent bacteria
10.1016/s0021-9258(18)32563-8 · 1983 · External reference
Indole-3-acetaldehyde dehydrogenase-dependent auxin synthesis contributes to virulence of Pseudomonas syringae strain DC3000
10.1371/journal.ppat.1006811 · 2018 · External reference
Structural basis of substrate recognition by aldehyde dehydrogenase 7A1
10.1021/acs.biochem.5b00754 · 2015 · External reference
