PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20155941-4 2010 Normal coordinate structural decomposition (NSD) of the ferric CBS crystal structure predicts the enhancement of normal modes with significant heme "doming", "ruffling", and "saddling" content, and they are observed in the coherence spectra near approximately 40, approximately 60, and approximately 90 cm(-1). Ferric enterobactin ion 56-62 cystathionine beta-synthase Homo sapiens 63-66 20155941-6 2010 For ferric CBS, we observe a new mode near approximately 25 cm(-1), possibly involving the response of the protein, which exhibits a phase jump of approximately pi for excitation on the blue and red side of the Soret band maximum. Ferric enterobactin ion 4-10 cystathionine beta-synthase Homo sapiens 11-14 15544339-5 2004 Instead, pH was found to control the equilibrium amount of ferric and ferrous heme present after reaction of CBS with one-electron reducing agents. Ferric enterobactin ion 59-65 cystathionine beta-synthase Homo sapiens 109-112 11148040-5 2001 In this study, we have characterized the heme cofactor of CBS in both the ferric and ferrous states using resonance Raman spectroscopy. Ferric enterobactin ion 74-80 cystathionine beta-synthase Homo sapiens 58-61 21875066-2 2011 The presence of a heme cofactor in CBS is enigmatic, and its conversion from the ferric- to ferrous-CO state inhibits enzyme activity. Ferric enterobactin ion 81-87 cystathionine beta-synthase Homo sapiens 35-38