Identification of the fifth axial heme ligand of chloroperoxidase.

Chemistry

• Primary Structure 100%
• Cysteine 100%
• Heme 100%
• Cysteine Residue 100%
• Reversed Phase HPLC 100%
• 2-Nitrobenzoic Acid 100%
• Disulfide 50%
• Amino Acid 50%
• Cytochrome 50%
• Substance Spectroscopy 50%
• Apoprotein 50%
• Protein Hydrolysis 50%

Keyphrases

• Chloroperoxidase 100%
• Heme Ligand 100%
• Cysteine 28%
• Sequence Analysis 28%
• Axial Ligand 28%
• Cysteine Residues 28%
• Reversed-phase HPLC 28%
• Ellman's Reagent 28%
• Denaturing Conditions 28%
• 5,5′-dithiobis(2-nitrobenzoic acid) 28%
• Amino Acids 14%
• Spectroscopic Data 14%
• Incubation 14%
• In(III) 14%
• Thiolate 14%
• Unique Peptide 14%
• Reducing Conditions 14%
• Resonance Raman 14%
• Labeled Peptide 14%
• Caldariomyces Fumago 14%
• Apoprotein 14%
• Digestion 14%
• Disulfide Linkage 14%
• Raman Studies 14%
• Active Site Structure 14%
• Cytochrome 14%
• Proteolysis 14%
• Endoproteinase 14%
• Gluc 14%
• Protoporphyrin IX (PpIX) 14%
• Acceptor Molecules 14%
• Substituted Enzyme 14%
• Chlorination 14%
• Peroxidative 14%
• Organic Acceptors 14%
• Cysteine-rich Peptides 14%

Pharmacology, Toxicology and Pharmaceutical Science

• Chloride Peroxidase 100%
• Heme 100%
• Cysteine 57%
• Reverse Phase High Performance Liquid Chromatography 28%
• 5,5' Dithiobis(2 Nitrobenzoic Acid) 28%
• Ellman's Reagent 28%
• Disulfide 14%
• Amino Acid 14%
• Apoprotein 14%
• Thiolates 14%
• Hematin 14%
• Cytochrome 14%