A synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolism.

ABSTRACT:

Background

FeFe-hydrogenases are the most active class of H2-producing enzymes known in nature and may have important applications in clean H2 energy production. Many potential uses are currently complicated by a crucial weakness: the active sites of all known FeFe-hydrogenases are irreversibly inactivated by O2.

Results

We have developed a synthetic metabolic pathway in E. coli that links FeFe-hydrogenase activity to the production of the essential amino acid cysteine. Our design includes a complementary host strain whose endogenous redox pool is insulated from the synthetic metabolic pathway. Host viability on a selective medium requires hydrogenase expression, and moderate O2 levels eliminate growth. This pathway forms the basis for a genetic selection for O2 tolerance. G

SUBMITTER: Barstow B 

PROVIDER: S-EPMC3130634 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature