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Combinatorial Synthesis of Four‐Helix Bundle Hemoproteins for Tuning of Cofactor Properties
Author(s) -
Rau Harald K.,
DeJonge Niels,
Haehnel Wolfgang
Publication year - 2000
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(20000103)39:1<250::aid-anie250>3.0.co;2-v
Subject(s) - antiparallel (mathematics) , helix bundle , hemeprotein , chemistry , cofactor , peptide , myoglobin , redox , protoporphyrin , stereochemistry , amino acid , crystallography , heme , protein structure , biochemistry , porphyrin , enzyme , inorganic chemistry , physics , quantum mechanics , magnetic field
Abstract De novo proteins were assembled from two sets of helical peptides on cyclic peptide templates bound to cellulose membranes (see picture). The variation of the amino acids of the hydrophobic binding pocket in the antiparallel four‐helix bundle tuned the redox potential of the reversibly bound Fe III – protoporphyrin IX group, as directly detected spectroscopically on the solid support.