Biochemistry and Physiology of Bioluminescent Bacteria

Hastings, J. Woodland; Potrikus, C. J.; Gupta, Srishti; Kurfürst, Manfred; Makemson, John C.

doi:10.1016/s0065-2911(08)60398-7

Cited by 199 publications

(115 citation statements)

References 188 publications

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“…Similarly, luxAB reporter gene cassettes sourced from various bioluminescent donors function in a wide range of host organisms, again exploiting one or more FR activities of the hosts (Hastings et al 1985;Meighen 1991). Another reflexion of this relaxed specificity is the preparation of highly active 'fused' flavin monooxygenases that has been reported.…”

Section: Discussionmentioning

confidence: 99%

“…A number of MCMOs play important roles as biocatalysts in commercially important biotechnological applications. This includes the hydroxylase from Streptomyces carbophilus SANK 62585 employed for the bioconversion of mevastatin into the widely used hypocholestemic drug pravastatin (Matsuoka et al 1989;Serizawa and Matsuoka 1991) and a number of luciferases exploited both directly and indirectly in various applications due to their characteristic bioluminescent properties (Hastings et al 1985;Meighen 1991).…”

Section: Introductionmentioning

confidence: 99%

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Functional assembly of camphor converting two-component Baeyer–Villiger monooxygenases with a flavin reductase from E. coli

Kadow

Balke

Willetts³

et al. 2013

Appl Microbiol Biotechnol

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Functional assembly of camphor converting two-component Baeyer–Villiger monooxygenases with a flavin reductase from E. coli

Kadow

Balke

Willetts³

et al. 2013

Appl Microbiol Biotechnol

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“…The bacterial luciferase has been studied most intensively in these organisms from a variety of viewpoints (Hastings, Potrikus, Gupta, Kurfurst & Makemson, 1985;Meighen, 1991;Baldwin & Ziegler, 1992). The in vitro lightemitting reaction scheme has been established as,…”

Section: Introductionmentioning

confidence: 99%

Structure of flavoprotein FP390 from a luminescent bacterium Photobacterium phosphoreum refined at 2.7 Å resolution

Kita

Kasai²,

Miyata³

et al. 1996

Acta Crystallogr D Biol Crystallogr

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The three-dimensional structure of a flavoprotein, FP~,~o, from a luminescent bacterium, Photobacterium phosphoreum, solved by the molecular-replacement method, was refined to an R factor of 24.0% for 17433 independent reflections, from 6.0 to 2.7~, resolution, collected by synchrotron radiation. The asymmetric unit of the crystal (space group P4322, a=b=76.8 and c --242 A) contains two monomer molecules related by a non-crystallographic twofold axis to form a dimer. There are two Q-flavin [flavin mononucleotide (FMN) with myristic acid] molecules in FP3,~o monomer. One of them is located at the interface of dimer which is bound to both monomer and the another is at the molecular surface. The electron density of myristic acids of Qflavins at the dimer interface in both monomer are weak and unclear, showing the possibility that the Q-flavins bound in this site are not a single species but a mixture of two components, 6-(3"-myristic acid)-FMN and 6-(4"-myristic acid)-FMN.

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“…In a previous communication we have reported the occurrence of a further intermediate The luciferase in bioluminescent bacteria is a having a similar fluoresence, which occurs subse flavinmonooxygenase which, in the course of quent to light emission in spent reaction mixtures activating molecular oxygen and oxidizing a long [5]. Its chromophore was proposed to be the chain aldehyde, emits light (A max = 490 nm) [1].…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction

Kurfuerst¹,

Macheroux²,

Ghisla³

et al. 1987

Biochimica et Biophysica Acta (BBA) - General Subjects

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Procedures and conditions have been established such that the unstable enzyme-bound flavin intermediate produced in the bacterial luciferase reacti~ can be isolated as approximately 70% of the flavin product, the remaining being the final product, FMN. The structure of the intermediate is proposed to be that of a luciferase-bound 4a,5-dihydroflavin-4a-hydroxide. The intermediate has a half-life of 33 min at 2° C and decays spontaneously to give H 2 0 and luciferase-bound FMN with an activation enthalpy of about 120 kJ Imo!. It has an absorption spectrum (A max = 360 nm) that is consistent with the proposed structure, and a fluorescence emission (A max =485 nm) that matches the bioluminescence emission closely.

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Biochemistry and Physiology of Bioluminescent Bacteria

Cited by 199 publications

References 188 publications

Functional assembly of camphor converting two-component Baeyer–Villiger monooxygenases with a flavin reductase from E. coli

Functional assembly of camphor converting two-component Baeyer–Villiger monooxygenases with a flavin reductase from E. coli

Structure of flavoprotein FP390 from a luminescent bacterium Photobacterium phosphoreum refined at 2.7 Å resolution

Isolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction

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