Skip to search formSkip to main contentSkip to account menu

heme binding

Known as: haem binding 
Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring. [CHEBI:30413, GOC:ai]
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2011
Highly Cited
2011
This study establishes that plant TSPO, an enigmatic stress-induced membrane protein, binds porphyrins, including heme in vitro… 
Highly Cited
2010
Highly Cited
2010
BackgroundHeme is an essential molecule and plays vital roles in many biological processes. The structural determination of a… 
Highly Cited
2010
Highly Cited
2010
Rev-erbβ is a heme-binding nuclear hormone receptor that represses a broad spectrum of target genes involved in regulating… 
Highly Cited
2009
Highly Cited
2009
The principles of natural protein engineering are obscured by overlapping functions and complexity accumulated through natural… 
Highly Cited
2007
Highly Cited
2007
Successful pathogenic organisms have developed mechanisms to thrive under extreme levels of iron restriction. Haem‐iron… 
Highly Cited
2007
Highly Cited
2007
TyrA is a member of the dye‐decolorizing peroxidase (DyP) family, a new family of heme‐dependent peroxidase recently identified… 
Highly Cited
2005
Highly Cited
2005
The acquisition of iron is essential for the survival of pathogenic bacteria, which have consequently evolved a wide variety of… 
Highly Cited
2003
Highly Cited
2003
HasA(SM) secreted by the Gram-negative bacterium Serratia marcescens belongs to the hemophore family. Its role is to take up heme… 
Review
2002
Review
2002
Post-translational maturation of c-type cytochromes involves covalent attachment of haem to the apocytochrome polypeptide by two… 
Highly Cited
2001
Highly Cited
2001
Haem binding to human serum albumin (HSA) endows the protein with peculiar spectroscopic properties. Here, the effect of…