Resonance Raman characterization of the heme cofactor in cystathionine beta-synthase. Identification of the Fe-S(Cys) vibration in the six-coordinate low-spin heme.
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Modulation of cystathionine beta-synthase activity by the Arg-51 and Arg-224 mutationsSpectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: nature of the ferrous and ferric cysteine adducts and mechanistic implications.Neutral thiol as a proximal ligand to ferrous heme iron: implications for heme proteins that lose cysteine thiolate ligation on reduction.Reversible heme-dependent regulation of human cystathionine β-synthase by a flavoprotein oxidoreductase.Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme.Identification of Cys94 as the distal ligand to the Fe(III) heme in the transcriptional regulator RcoM-2 from Burkholderia xenovorans.Allosteric communication between the pyridoxal 5'-phosphate (PLP) and heme sites in the H2S generator human cystathionine β-synthase.Effect of the disease-causing R266K mutation on the heme and PLP environments of human cystathionine β-synthase.Properties of an unusual heme cofactor in PLP-dependent cystathionine beta-synthase.Heme regulation of human cystathionine beta-synthase activity: insights from fluorescence and Raman spectroscopy.Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation.Investigations of low-frequency vibrational dynamics and ligand binding kinetics of cystathionine beta-synthase.The transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch.Nuclear receptors homo sapiens Rev-erbbeta and Drosophila melanogaster E75 are thiolate-ligated heme proteins which undergo redox-mediated ligand switching and bind CO and NO.Hydrogen Sulfide Oxidation by Myoglobin.Pyridoxal phosphate binding sites are similar in human heme-dependent and yeast heme-independent cystathionine beta-synthases. Evidence from 31P NMR and pulsed EPR spectroscopy that heme and PLP cofactors are not proximal in the human enzyme.Potential Pharmacological Chaperones for Cystathionine Beta-Synthase-Deficient Homocystinuria.Chemical Biology of H2S Signaling through Persulfidation.
P2860
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P2860
Resonance Raman characterization of the heme cofactor in cystathionine beta-synthase. Identification of the Fe-S(Cys) vibration in the six-coordinate low-spin heme.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Resonance Raman characterizati ...... se. Identification of the Fe-S
@nl
Resonance Raman characterizati ...... six-coordinate low-spin heme.
@en
type
label
Resonance Raman characterizati ...... se. Identification of the Fe-S
@nl
Resonance Raman characterizati ...... six-coordinate low-spin heme.
@en
prefLabel
Resonance Raman characterizati ...... se. Identification of the Fe-S
@nl
Resonance Raman characterizati ...... six-coordinate low-spin heme.
@en
P2093
P356
P1433
P1476
Resonance Raman characterizati ...... six-coordinate low-spin heme.
@en
P2093
P304
P356
10.1021/BI0010874
P407
P577
2001-01-01T00:00:00Z