Mercuric chloride-induced spin or ligation state changes in ferric or ferrous human cystathionine β-synthase inhibit enzyme activity
- 15 December 2001
- journal article
- Published by Elsevier in Journal of Inorganic Biochemistry
- Vol. 87 (4) , 253-259
- https://doi.org/10.1016/s0162-0134(01)00336-1
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Characterization of NO binding to human cystathionine β-synthase:Journal of Inorganic Biochemistry, 2001
- Resonance Raman Characterization of the Heme Cofactor in Cystathionine β-Synthase. Identification of the Fe−S(Cys) Vibration in the Six-Coordinate Low-Spin HemeBiochemistry, 2000
- Characterization of the Heme in Human Cystathionine β-Synthase by X-ray Absorption and Electron Paramagnetic Resonance SpectroscopiesBiochemistry, 2000
- Yeast Cystathionine β-Synthase Is a Pyridoxal Phosphate Enzyme but, Unlike the Human Enzyme, Is Not a Heme ProteinJournal of Biological Chemistry, 2000
- Characterization of the Heme and Pyridoxal Phosphate Cofactors of Human Cystathionine β-Synthase Reveals Nonequivalent Active SitesBiochemistry, 1999
- Folate, Vitamin B12, and Serum Total Homocysteine Levels in Confirmed Alzheimer DiseaseArchives of Neurology, 1998
- Evidence for Heme-mediated Redox Regulation of Human Cystathionine β-Synthase ActivityJournal of Biological Chemistry, 1998
- Homocysteine and Cardiovascular DiseaseAnnual Review of Medicine, 1998
- Irreversible Inhibition of Lysyl Oxidase by Homocysteine Thiolactone and Its Selenium and Oxygen AnaloguesJournal of Biological Chemistry, 1997
- Homocysteine metabolism in pregnancies complicated by neural-tube defectsThe Lancet, 1995