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Characterization of a de novo Designed Heme Protein by EPR and ENDOR Spectroscopy
Author(s) -
Fahnenschmidt M.,
Rau H. K.,
Bittl R.,
Haehnel W.,
Lubitz W.
Publication year - 1999
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/(sici)1521-3765(19990802)5:8<2327::aid-chem2327>3.0.co;2-k
Subject(s) - electron paramagnetic resonance , heme , hemeprotein , metmyoglobin , cofactor , imidazole , chemistry , stereochemistry , protein design , biochemistry , protein structure , nuclear magnetic resonance , myoglobin , enzyme , physics
Binding pockets for cofactors can be built with de novo designed proteins. A modular protein (shown here) synthesized according to the design concept of a template‐assembled synthetic protein that accomodates two heme groups is studied. The details of the binding situation of the heme groups are investigated by EPR and electron nuclear double resonance (ENDOR) techniques. Similarities to the binding situation in metmyoglobin–imidazole are discussed.