Shapes and Patterns of Heme-Binding Motifs in Mammalian Heme-Binding Proteins

Ligand Binding to Heme Proteins

The 02, CO, and alkyl isocyanide-binding properties of a variety of vertebrate and invertebrate heme proteins have been compared in detail to those of protoheme mOn0-3-( 1-imidazoy1)-propylamide monomethyl ester in aqueous suspensions of soap micelles. The proteins examined include: cytochrome P-450,,, from Pseudomonasputida, beef heart cytochrome c oxidase, yeast cytochrome c peroxidase, a and...

Diversity and conservation of interactions for binding heme in b-type heme proteins.

SIAA and Neat2 Heme Binding Proteins from Streptococcus Pyogenes

The bacterium Streptococcus pyogenes requires heme, which is taken up via an ABC transporter. An understanding of this pathway may result in new approaches to antibacterial agents. Both SiaA and NEAT2 (NEAr Transporter 2) are proteins involved in heme binding. One of the axial ligands of SiaA, His 229, was purified to study how mutagenesis affects heme binding. UVvisible studies showed a small ...

Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins.

We investigated the ultrafast structural transitions of the heme induced by nitric oxide (NO) binding for several heme proteins by subpicosecond time-resolved resonance Raman and femtosecond transient absorption spectroscopy. We probed the heme iron motion by the evolution of the iron-histidine Raman band intensity after NO photolysis. Unexpectedly, we found that the heme response and iron moti...

Unusual heme-binding PAS domain from YybT family proteins.

YybT family proteins (COG3887) are functionally unknown proteins that are widely distributed among the firmicutes, including the human pathogens Staphylococcus aureus and Listeria monocytogenes. Recent studies suggested that YybT family proteins are crucial for the in vivo survival of bacterial pathogens during host infection. YybT family proteins contain an N-terminal domain that shares minimu...