Abstract
Carbon monoxide dehydrogenase (CODH) isolated from the photosynthetic bacterium Rhodospirillum rubrum is an oxygen-labile enzyme that catalyzes the reversible oxidation of CO to CO2. The presence of CODH allows R. rubrum to grow anaerobically in the dark with CO as sole energy source. Spectroscopic and crystallographic studies have shown that the active site for CO oxidation is an unprecedented Ni-Fe-S metallocluster (referred to as the C-cluster). The goals of this research project have been: (1) to study the assembly of the active site C-cluster of CODH, (2) to determine the mechanism of CO oxidation by R. rubrum CODH in the context of the structure of the enzyme and, (3) to study the properties of CODH bound to its physiological electron acceptor protein, CooF. A combined genetic and biochemical approach has been used to address these questions.
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