Catalytic iron-carbene intermediate revealed in a cytochrome c carbene transferase.

ABSTRACT: Recently, heme proteins have been discovered and engineered by directed evolution to catalyze chemical transformations that are biochemically unprecedented. Many of these nonnatural enzyme-catalyzed reactions are assumed to proceed through a catalytic iron porphyrin carbene (IPC) intermediate, although this intermediate has never been observed in a protein. Using crystallographic, spectroscopic, and computational methods, we have captured and studied a catalytic IPC intermediate in the active site of an enzyme derived from thermostable Rhodothermus marinus (Rma) cytochrome c High-resolution crystal structures and computational methods reveal how directed evolution created an active site for carbene transfer in an electron transfer protein and how the laboratory-evolved

SUBMITTER: Lewis RD 

PROVIDER: S-EPMC6048479 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature