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1 Introduction Photocatalysis is a very common principle in nature: All plants and animals depend on sunlight and use it by means of photoreceptors. One of the most prominent examples of photoreceptor dyes is riboflavin (RF), also known as vitamin B 2 , which takes part in biochemical redox reactions as a coenzyme [ 1 ]. Besides their role as photoreceptor dyes [ 2 ], the photoactivity of flavins is crucial for some other natural processes, e. g. the light generation by bacterial luciferase [ 3 ], and DNA repair by photolyase [ 4 ]. RF and its derivatives are

1032 W.-R. KNAPPE AND P. HEMMERICH Covalent Intermediates in Flavin-sensitized Photodehydrogenation and Photodecarboxylation W . - R . KNAPPE a n d P . HEMMERICH Department of Biology, University of Konstanz, Germany (Z. Naturforsch. 27 b , 1032—1035 [1972] ; received May 10, 1972) Covalent Photoadducts of Flavins The photoreactions of the flavin triplet with unsaturated hydrocarbons, aldehydes, sulphur compounds, and carbonic acids are reported. These reactions proceed by attack at the allylic C —H-, the RCO —H-, or the a-C —H-bond, respectively; in the

Burkhard König, Susanne Kümmel, Eva Svobodová and Radek Cibulka 3 Flavin photocatalysis Abstract: Thanks to rapid development in the last decades, flavins have been recog- nized as promising photoactive compounds to design new valuable synthetic method- ologies based on photoredox catalysis. The review summarizes general photochemical properties of flavins as well as their early applications in transformations mediated by visible light. Special attention has been paid to the catalyst design for benzylic oxida- tions as well as to recent flavin applications, for

2′-Oxoethyl Flavin Revisited Jiřı́ Svobodaa, Burkhard Königa, Keyarash Sadeghianb, and Martin Schützb a Institute of Organic Chemistry, University Regensburg, D-93040 Regensburg, Germany b Institute of Physical and Theoretical Chemistry, University Regensburg, D-93040 Regensburg, Germany Reprint requests to Prof. B. König. E-mail: burkhard.koenig@chemie.uni-regensburg.de Z. Naturforsch. 2008, 63b, 47 – 54; received August 3, 2007 The present work investigates the possibility of using 2′-oxoethyl flavin (2) as a starting material for the construction of more

FLAVIN-BENZIMIDAZOL-DINUCLEOTID 1149 Darstellung und Eigenschaften von Flavin-benzimidazol-dinucleotid P . ZüMPE u n d C. WOENCKHAUS Institut für Biochemie im Institut für Organische Chemie der Universität Frankfurt/Main (Z. Naturforschg. 21 b, 1149—1152 [1966] ; eingegangen am 31. Mai 1966) Die Synthese des Coenzymmodells Flavin-benzimidazol-dinucleotid * gelang durch Kondensation von Benzimidazolribotid-imidazolid 1 oder Benzimidazolribotid-guanidiniumamidat 2 mit Flavinmono- nucleotid. Das Coenzymmodell war enzymatisch nicht aktiv und bildete keinen Enzym

BAND 27 I. ZEITSCHRIFT FÜR NATURFORSCHUNG HEFT 9 M o l e c u l a r L u m i n e s c e n c e Studies o f F lav ins , I I Interactions Involving the Excited States * PILL-SOON SONG, THOMAS A . MOORE, and WILLIAM E . KURTIN * * Department of Chemistry, Texas Tech University, Lubbock, Texas 79409 (Z. Naturforsch. 27 b, 1011—1015 [1972] ; received May 10, 1972) Polarization of flavins, Flavin dimers, Alloxazine-KI charge transfer states, Energy Transfer The effects of experimental geometry on the theoretical polarizations of the S t S0 and S2 <— S0 bands of

Proceedings of the Tenth International Symposium, Como, Italy, July 15–20, 1990
Proceedings of the Eighth International Symposium, Brighton, England, July 9–13, 1984
Proceedings of the Ninth International Symposium, Atlanta, Georgia, USA, June 7–12, 1987

COVALENTLY BOUND FLAVIN COENZYMES 1 0 6 9 Recent Advances in the Chemistry of Covalently Bound Flavin Coenzymes W . C . KENNEY, W . H . WALKER, E. B . KEARNEY, R . SENG, a n d T . P . SINGER Department of Biochemistry and Biophysics, University of California, San Francisco, California 94122 and Molecular Biology Division, Veterans Administration Hospital, San Francisco, California 94121, U.S.A. and J . R . CRONIN a n d R . HENDRIKS Department of Chemistry, Arizona State University, Tempe, Arizona 85281, U.S.A. (Z. Naturforsch. 27 b, ]069—1071 [1972