The heme of cystathionine beta-synthase likely undergoes a thermally induced redox-mediated ligand switch.
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Crystal structure at 1.5Å resolution of the PsbV2 cytochrome from the cyanobacterium Thermosynechococcus elongatusRescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: purification and characterization of eight CBS mutant enzymes.Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2.Purification and characterization of cystathionine β-synthase bearing a cobalt protoporphyrin.PLP-dependent H(2)S biogenesis.Folding and activity of mutant cystathionine β-synthase depends on the position and nature of the purification tag: characterization of the R266K CBS mutantAllosteric 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.Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase.Properties of an unusual heme cofactor in PLP-dependent cystathionine beta-synthase.Kinetics of reversible reductive carbonylation of heme in human cystathionine β-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.Inactivation of cystathionine beta-synthase with peroxynitrite.Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.The bacterial SoxAX cytochromes.Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone.Comparative study of enzyme activity and heme reactivity in Drosophila melanogaster and Homo sapiens cystathionine β-synthases.Cobalt cystathionine β-synthase: a cobalt-substituted heme protein with a unique thiolate ligation motif.Potential Pharmacological Chaperones for Cystathionine Beta-Synthase-Deficient Homocystinuria.Chemical Biology of H2S Signaling through Persulfidation.Redox and metal-regulated oligomeric state for human porphobilinogen synthase activation.
P2860
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P2860
The heme of cystathionine beta-synthase likely undergoes a thermally induced redox-mediated ligand switch.
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The heme of cystathionine beta ...... redox-mediated ligand switch.
@ast
The heme of cystathionine beta ...... redox-mediated ligand switch.
@en
type
label
The heme of cystathionine beta ...... redox-mediated ligand switch.
@ast
The heme of cystathionine beta ...... redox-mediated ligand switch.
@en
prefLabel
The heme of cystathionine beta ...... redox-mediated ligand switch.
@ast
The heme of cystathionine beta ...... redox-mediated ligand switch.
@en
P2093
P356
P1433
P1476
The heme of cystathionine beta ...... redox-mediated ligand switch.
@en
P2093
Gudrun S Lukat-Rodgers
Jan P Kraus
Jana Oliveriusová
Judith N Burstyn
Kenton R Rodgers
Melisa M Cherney
Samuel Pazicni
P304
16785-16795
P356
10.1021/BI051305Z
P407
P577
2005-12-01T00:00:00Z