Article
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.
Journal of inorganic biochemistry - 1 May 2009
Singh Sangita, Madzelan Peter, Stasser Jay, Weeks Colin L, Becker Donald, Spiro Thomas G, Penner-Hahn James, Banerjee Ruma
Abstract excerpt
In humans, cystathionine beta-synthase (CBS) is a hemeprotein, which catalyzes a pyridoxal phosphate (PLP)-dependent condensation reaction. Changes in the heme environment are communicated to the active site, which is approximately 20A away. In this study, we have examined the role of H67 and R266, which are in the second coordination sphere of the heme ligands, H65 and C52, respectively, in modulating the heme's...
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