Abstract
Dark-operative protochlorophyllide oxidoreductase (DPOR) is a nitrogenase-like enzyme consisting of two components, L-protein as a reductase component and NB-protein as a catalytic component. Elucidation of the crystal structures of NB-protein (Muraki et al., Nature 2010, 465: 110-114) has enabled us to study its reaction mechanism in combination with biochemical analysis. Here we demonstrate that nicotinamide (NA) inhibits DPOR activity by blocking the electron transfer from L-protein to NB-protein. A reaction scheme of DPOR, in which the binding of protochlorophyllide (Pchlide) to the NB-protein precedes the electron transfer from the L-protein, is proposed based on the NA effects.
Original language | English |
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Pages (from-to) | 3142-3147 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 587 |
Issue number | 18 |
DOIs | |
Publication status | Published - 2013 Sept 17 |
Externally published | Yes |
Keywords
- Bacteriochlorophyll
- Chlorophyll
- FeS cluster
- Nitrogenase
- Protochlorophyllide
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology