کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2052101 | 1074221 | 2006 | 4 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Nitrogenase Fe protein-like Fe–S cluster is conserved in L-protein (BchL) of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus Nitrogenase Fe protein-like Fe–S cluster is conserved in L-protein (BchL) of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus](/preview/png/2052101.png)
Dark-operative protochlorophyllide reductase (DPOR) in bacteriochlorophyll biosynthesis is a nitrogenase-like enzyme consisting of L-protein (BchL-dimer) as a reductase component and NB-protein (BchN–BchB-heterotetramer) as a catalytic component. Metallocenters of DPOR have not been identified. Here we report that L-protein has an oxygen-sensitive [4Fe–4S] cluster similar to nitrogenase Fe protein. Purified L-protein from Rhodobacter capsulatus showed absorption spectra and an electron paramagnetic resonance signal indicative of a [4Fe–4S] cluster. The activity quickly disappeared upon exposure to air with a half-life of 20 s. These results suggest that the electron transfer mechanism is conserved in nitrogenase Fe protein and DPOR L-protein.
Journal: FEBS Letters - Volume 580, Issue 26, 13 November 2006, Pages 6151–6154