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Cover Feature: Structural Biology of Iron‐Binding Proteins by NMR Spectroscopy (Eur. J. Inorg. Chem. 5/2019)
Author(s) -
Ciambellotti Silvia,
Turano Paola
Publication year - 2019
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201900041
Subject(s) - chemistry , biomineralization , nanocages , nuclear magnetic resonance spectroscopy , biophysics , cover (algebra) , cytochrome , crystallography , heme , biochemistry , stereochemistry , chemical engineering , mechanical engineering , engineering , biology , enzyme , catalysis
The Cover Feature shows schematic sketches of biological processes, involving heme/iron‐binding proteins, studied by NMR spectroscopy. Mitochondrial cytochrome c presents distinct surface interaction areas when shuttling electrons between inner‐membrane respiratory complexes and interacting with antiapoptotic proteins such as Bcl‐xL. The hemophore protein HasA from Serratia marcescens can deliver heme upon binding to the external membrane receptor HasR. Iron pathways into the ferritin nanocage are relevant for protein‐assisted biomineralization. More information can be found in the Microreview by S. Ciambellotti and P. Turano .