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© Research
Publication : Archives of biochemistry and biophysics

Inactivation of cystathionine beta-synthase with peroxynitrite.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Archives of biochemistry and biophysics - 01 Nov 2009

Celano L, Gil M, Carballal S, Durán R, Denicola A, Banerjee R, Alvarez B,

Link to Pubmed [PMID] – 19733148

Link to DOI – 10.1016/j.abb.2009.08.022

Arch Biochem Biophys 2009 Nov; 491(1-2): 96-105

Cystathionine beta-synthase (CBS) is a homocysteine metabolizing enzyme that contains pyridoxal phosphate (PLP) and a six-coordinate heme cofactor of unknown function. CBS was inactivated by peroxynitrite, the product of nitric oxide and superoxide radicals. The IC(50) was approximately 150microM for 5microM ferric CBS. Stopped-flow kinetics and competition experiments showed a direct reaction with a second-order rate constant of (2.4-5.0)x10(4)M(-1)s(-1) (pH 7.4, 37 degrees C). The radicals derived from peroxynitrite, nitrogen dioxide and carbonate radical, also inactivated CBS. Exposure to peroxynitrite did not modify bound PLP but led to nitration of Trp208, Trp43 and Tyr223 and alterations in the heme environment including loss of thiolate coordination, conversion to high-spin and bleaching, with no detectable formation of oxo-ferryl compounds nor promotion of one-electron processes. This study demonstrates the susceptibility of CBS to reactive oxygen/nitrogen species, with potential relevance to hyperhomocysteinemia, a risk factor for cardiovascular diseases.

https://pubmed.ncbi.nlm.nih.gov/19733148