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Featured researches published by Manfred Kurfürst.


Advances in Microbial Physiology | 1985

Biochemistry and Physiology of Bioluminescent Bacteria

J. Woodland Hastings; Catherine J. Potrikusv; Subhash C. Gupta; Manfred Kurfürst; John C. Makemson

Publisher Summary This chapter describes the biochemistry and physiology of bioluminescent bacteria. The function of bioluminescent bacteria is to emit light in biological systems. The chapter explains the variety of habitats in which these bacteria are found, the light-emitting system may play an important role in their ecology or physiology. The luciferase in bacteria, unlike that of any other luminous group (except, perhaps, the fungi), is related to the respiratory pathway, functioning as a shunt for electrons directly to oxygen at the level of reduced flavin. This luciferase is an external flavin mono-oxygenase or mixed-function oxidase, electrons for reduction of flavin mononucleotide (FMN) are provided by the reducing power derived from the electron-transport pathway. The light-emitting reaction then proceeds via the reaction of molecular oxygen with reduced flavin to form an intermediate luciferase-flavin peroxy species, whose breakdown provides energy sufficient to leave one of the products in an electronically excited singlet state, with subsequent light emission. The bacterial (luciferase-bound) peroxide chromophore, which has been isolated and characterized, provides a model in this respect for the different bioluminescent reactions.


Bioluminescence and Chemiluminescence#R##N#Basic Chemistry and Analytical Applications | 1981

The Red Absorbing Flavin Species in the Reaction of Bacterial Luciferase with FMNH2 and O2

J. Woodland Hastings; Robert Presswood; Sandro Ghisla; Manfred Kurfürst; Peter Hemmerich

The reaction of luciferase-bound Z is known to result in the formation of a long-lived intermedlate in the bioluminescent reaction (1). This intermediate was isolated and ,haracterized as the luciferase-peroxyflavin (2), whose struc~ture was later shown to be the flavin 4a-substituted peroxyadduct (3). In the earlier work this peroxy intermediate had been shown to exhibit a single peak at about 370 rum, a shoulder a-t about 460 run, the absorption tailing off around 500 rum, with none above 520 run. In more recent publications,however (4,5), it has been reported that the reaction of the luciferase-bound reduced flavin mononucleotide with O2 also results in the appearance


FEBS Journal | 2001

L‐Amino‐acid oxidase from the Malayan pit viper Calloselasma rhodostoma

Peter Macheroux; Oliver Seth; Claus Bollschweiler; Margarete Schwarz; Manfred Kurfürst; Lo-Chun Au; Sandro Ghisla


FEBS Journal | 1982

Structure and Catalytic Inactivity of the Bacterial Luciferase Neutral Flavin Radical

Manfred Kurfürst; Sandro Ghisla; Robert Presswood; J. Woodland Hasttngs


Archive | 1989

Polypeptides with a prourokinase activity, their production and use.

Wolfgang Koerwer; Manfred Kurfürst; Verena Baldinger; Thomas Doerper; Margarete Schwarz


FEBS Journal | 1989

Bioluminescence emission of bacterial luciferase with 1-deaza-FMN Evidence for the noninvolvement of N(1)-protonated flavin species as emitters

Manfred Kurfürst; Peter Macheroux; Sandro Ghisla; J. Woodland Hastings


Archive | 1984

Identification of the Luciferase-Bound Flavin-4A-Hydroxide as the Primary Emitter in the Bacterial Bioluminescence Reaction

Manfred Kurfürst; J. Woodland Hastings; Sandro Ghisla


Bioluminescence and Chemiluminescence#R##N#Basic Chemistry and Analytical Applications | 1981

Fluorescence Properties of Luciferase Peroxyflavins Prepared with ISO-FMN and 2-THIO FMN

J. Woodland Hastings; Sandro Ghisla; Manfred Kurfürst; Peter Hemmerich


Flavins and flavoproteins | 1999

Studies on the glycosylation of L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma

Karina Kitzing; Michael Vetsch; Margarethe Sappelt; Sandro Ghisla; Margarete Schwarz; Manfred Kurfürst


Archive | 1982

The Bacterial Luciferase Neutral Flavin Radical : Identification and Catalytic Inactivity

Manfred Kurfürst; Sandro Ghisla; Robert Presswood; J. Woodland Hastings

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Karina Kitzing

Research Institute of Molecular Pathology

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Peter Macheroux

Graz University of Technology

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John C. Makemson

Florida International University

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